Structured Review

Millipore β lactoglobulin
( A – E ) AFM images of ( A ) multilamellar DMPG lipid bilayers, ( B ) multilamellar DMPG lipid bilayers, and adsorbed  β LG; ( C ) multilamellar DMPC lipid bilayers, ( D ) multilamellar DMPC lipid bilayers, and adsorbed  β LG; and ( E )  β LG adsorbed on to a Ge IRE surface. All images are shown on the same vertical scale for comparison purposes. ( F – J ) Simultaneously acquired ATR-FTIR spectra shown beside their corresponding AFM images. Scale bar: 0.2 absorbance units.
β Lactoglobulin, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Images

1) Product Images from "Tracking Molecular Interactions in Membranes by Simultaneous ATR-FTIR-AFM"

Article Title: Tracking Molecular Interactions in Membranes by Simultaneous ATR-FTIR-AFM

Journal: Biophysical Journal

doi: 10.1016/j.bpj.2009.06.013

( A – E ) AFM images of ( A ) multilamellar DMPG lipid bilayers, ( B ) multilamellar DMPG lipid bilayers, and adsorbed  β LG; ( C ) multilamellar DMPC lipid bilayers, ( D ) multilamellar DMPC lipid bilayers, and adsorbed  β LG; and ( E )  β LG adsorbed on to a Ge IRE surface. All images are shown on the same vertical scale for comparison purposes. ( F – J ) Simultaneously acquired ATR-FTIR spectra shown beside their corresponding AFM images. Scale bar: 0.2 absorbance units.
Figure Legend Snippet: ( A – E ) AFM images of ( A ) multilamellar DMPG lipid bilayers, ( B ) multilamellar DMPG lipid bilayers, and adsorbed β LG; ( C ) multilamellar DMPC lipid bilayers, ( D ) multilamellar DMPC lipid bilayers, and adsorbed β LG; and ( E ) β LG adsorbed on to a Ge IRE surface. All images are shown on the same vertical scale for comparison purposes. ( F – J ) Simultaneously acquired ATR-FTIR spectra shown beside their corresponding AFM images. Scale bar: 0.2 absorbance units.

Techniques Used:

2) Product Images from "Analysis and Comparison of Nutrition Profiles of Canine Milk with Bovine and Caprine Milk"

Article Title: Analysis and Comparison of Nutrition Profiles of Canine Milk with Bovine and Caprine Milk

Journal: Foods

doi: 10.3390/foods11030472

Reverse phase high-performance liquid chromatography chromatograms of protein fractions in canine, bovine, and caprine milk. α s1 -CN: α s1 -casein, α s2 -CN: α s2 -casein, β-CN: β-casein, κ-CN: κ-casein, β-LG: β-lactoglobulin, α-LA: α-lactalbumin.
Figure Legend Snippet: Reverse phase high-performance liquid chromatography chromatograms of protein fractions in canine, bovine, and caprine milk. α s1 -CN: α s1 -casein, α s2 -CN: α s2 -casein, β-CN: β-casein, κ-CN: κ-casein, β-LG: β-lactoglobulin, α-LA: α-lactalbumin.

Techniques Used: High Performance Liquid Chromatography

SDS-PAGE analysis of canine, bovine, and caprine milk. Lanes: M: Prestained protein molecular weight marker, (1) Holstein, (2) Saanen, (3) Golden Retriever, (4) Labrador, (5) Caucasian Sheepdog, (6) Rottweiler. LF: Lactoferrin, SA: Serum albumin, β-LG: β-lactoglobulin, LZ: Lysozyme, α-LA: α-lactalbumin, IgG: Immunoglobulin G, α s1 -CN: α s1 -casein, α s2 -CN: α s2 -casein, β-CN: β-casein, κ-CN: κ-casein.
Figure Legend Snippet: SDS-PAGE analysis of canine, bovine, and caprine milk. Lanes: M: Prestained protein molecular weight marker, (1) Holstein, (2) Saanen, (3) Golden Retriever, (4) Labrador, (5) Caucasian Sheepdog, (6) Rottweiler. LF: Lactoferrin, SA: Serum albumin, β-LG: β-lactoglobulin, LZ: Lysozyme, α-LA: α-lactalbumin, IgG: Immunoglobulin G, α s1 -CN: α s1 -casein, α s2 -CN: α s2 -casein, β-CN: β-casein, κ-CN: κ-casein.

Techniques Used: SDS Page, Molecular Weight, Marker

3) Product Images from "A Solid-in-Oil Nanodispersion System for Transcutaneous Immunotherapy of Cow’s Milk Allergies"

Article Title: A Solid-in-Oil Nanodispersion System for Transcutaneous Immunotherapy of Cow’s Milk Allergies

Journal: Pharmaceutics

doi: 10.3390/pharmaceutics12030205

Characterization of the solid-in-oil (S/O) nanodispersions with and without R-848. ( a ) Particle size distribution; ( b ) β-lactoglobulin (BLG) release test.
Figure Legend Snippet: Characterization of the solid-in-oil (S/O) nanodispersions with and without R-848. ( a ) Particle size distribution; ( b ) β-lactoglobulin (BLG) release test.

Techniques Used:

4) Product Images from "Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Traveling Wave Device"

Article Title: Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Traveling Wave Device

Journal: Analytical Chemistry

doi: 10.1021/acs.analchem.8b05641

Mass spectra for the proteins (A) Cytochrome C (CytC), (B) β-Lactoglobulin (βLac), and (C) Concanavalin A (ConA). Blue circle = monomer, green square = dimer, red triangle = tetramer.
Figure Legend Snippet: Mass spectra for the proteins (A) Cytochrome C (CytC), (B) β-Lactoglobulin (βLac), and (C) Concanavalin A (ConA). Blue circle = monomer, green square = dimer, red triangle = tetramer.

Techniques Used:

5) Product Images from "Protein Conformation in Amorphous Solids by FTIR and by Hydrogen/Deuterium Exchange with Mass Spectrometry"

Article Title: Protein Conformation in Amorphous Solids by FTIR and by Hydrogen/Deuterium Exchange with Mass Spectrometry

Journal: Biophysical Journal

doi: 10.1529/biophysj.108.139899

β -Lactoglobulin conformation in amorphous solids containing various additives (1:1 w/w). ( A ) Second derivative FTIR spectra. ( B ) ssHDX of intact protein. ( C ) ssHDX of peptic digests. Additives were Tre, Raf, dex, PVA, PVP, and Gdn. In  C , peptic
Figure Legend Snippet: β -Lactoglobulin conformation in amorphous solids containing various additives (1:1 w/w). ( A ) Second derivative FTIR spectra. ( B ) ssHDX of intact protein. ( C ) ssHDX of peptic digests. Additives were Tre, Raf, dex, PVA, PVP, and Gdn. In C , peptic

Techniques Used:

6) Product Images from "Anti-Inflammatory and Antioxidant Properties of Peptides Released from β-Lactoglobulin by High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis"

Article Title: Anti-Inflammatory and Antioxidant Properties of Peptides Released from β-Lactoglobulin by High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis

Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

doi: 10.3390/molecules22060949

( A ) Viability of RAW 264.7 cells; ( B ) Nitric oxide content of RAW 264.7 cell supernatant and ( C ) mRNA expression of pro-inflammatory cytokines (tumor necrosis factor (TNF-α) and IL-1β) relative to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (∆∆C t ) in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells in the presence of intact β-lactoglobulin (BLG) and BLG hydrolysates produced by alcalase under HHP and AP conditions (BLG-HHP-Alc and BLG-AP-Alc). The Negative Control indicates the cells grown without any treatment. The Positive Control indicates the cells treated with LPS, without treatment. The bars and error bars represent means and standard errors, respectively ( n ≥ 3). Means with different lowercase letters differ significantly ( p
Figure Legend Snippet: ( A ) Viability of RAW 264.7 cells; ( B ) Nitric oxide content of RAW 264.7 cell supernatant and ( C ) mRNA expression of pro-inflammatory cytokines (tumor necrosis factor (TNF-α) and IL-1β) relative to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (∆∆C t ) in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells in the presence of intact β-lactoglobulin (BLG) and BLG hydrolysates produced by alcalase under HHP and AP conditions (BLG-HHP-Alc and BLG-AP-Alc). The Negative Control indicates the cells grown without any treatment. The Positive Control indicates the cells treated with LPS, without treatment. The bars and error bars represent means and standard errors, respectively ( n ≥ 3). Means with different lowercase letters differ significantly ( p

Techniques Used: Expressing, Produced, Negative Control, Positive Control

SDS-PAGE on 12% polyacrylamide Tris-Tricine gels. BLG hydrolysates were produced under atmospheric ( A ) and high hydrostatic pressure ( B ) with various enzymes (neutrase (Neu), alcalase (Alc), savinase (Sav), elastase (Ela), thermolysin (Ther), and trypsin (Try); M , standard marker; C, unhydrolyzed β-lactoglobulin (BLG).
Figure Legend Snippet: SDS-PAGE on 12% polyacrylamide Tris-Tricine gels. BLG hydrolysates were produced under atmospheric ( A ) and high hydrostatic pressure ( B ) with various enzymes (neutrase (Neu), alcalase (Alc), savinase (Sav), elastase (Ela), thermolysin (Ther), and trypsin (Try); M , standard marker; C, unhydrolyzed β-lactoglobulin (BLG).

Techniques Used: SDS Page, Produced, Marker

The antioxidant capacity of selected β-lactoglobulin hydrolysates produced under HHP and AP condition. ( A ) DPPH scavenging capacity; ( B ) iron chelation capacity and ( C ) ferric reducing antioxidant power (FRAP) values of β-lactoglobulin hydrolysates produced by Alcalase (Alc), Thermolysin (Ther), and Savinase (Sav). The statistical analysis of the results was performed by two-way ANOVA followed by a Duncan multiple comparisons test. The bars and error bars represent means and standard errors, respectively ( n ≥ 3). For each concentration level, means with different lowercase letters differ significantly ( p
Figure Legend Snippet: The antioxidant capacity of selected β-lactoglobulin hydrolysates produced under HHP and AP condition. ( A ) DPPH scavenging capacity; ( B ) iron chelation capacity and ( C ) ferric reducing antioxidant power (FRAP) values of β-lactoglobulin hydrolysates produced by Alcalase (Alc), Thermolysin (Ther), and Savinase (Sav). The statistical analysis of the results was performed by two-way ANOVA followed by a Duncan multiple comparisons test. The bars and error bars represent means and standard errors, respectively ( n ≥ 3). For each concentration level, means with different lowercase letters differ significantly ( p

Techniques Used: Produced, Concentration Assay

The degree of hydrolysis of β-lactoglobulin (BLG) hydrolyzed under atmospheric (AP) and high hydrostatic pressure (HHP) at an enzyme-to-substrate (E:S) ratio of 1:100. The statistical analysis of the results was performed by two-way ANOVA followed by a Duncan multiple comparisons test. The bars and error bars represent means and standard errors, respectively ( n ≥ 3). Means with different lowercase letters differ significantly ( p
Figure Legend Snippet: The degree of hydrolysis of β-lactoglobulin (BLG) hydrolyzed under atmospheric (AP) and high hydrostatic pressure (HHP) at an enzyme-to-substrate (E:S) ratio of 1:100. The statistical analysis of the results was performed by two-way ANOVA followed by a Duncan multiple comparisons test. The bars and error bars represent means and standard errors, respectively ( n ≥ 3). Means with different lowercase letters differ significantly ( p

Techniques Used:

7) Product Images from "Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry"

Article Title: Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry

Journal: The Analyst

doi: 10.1039/c5an01819f

Fractional abundances of the a ions from the N-terminal portion of β-lactoglobulin for a) completely oxidized, b) source activated (50V), and c) partially reduced and source activated β-lactoglobulin. The crystal structure of β-lactoglobulin is shown from two different perspectives in d) and e), with the experimental protonation sites associated with the more native structure highlighted in red and the protonation sites associated with the more unfolded structure shown in blue. Dotted spheres indicate the solvent accessibility of the protein and disulfide bonds are highlighted in yellow. *The relative abundance of fragments increased by 10-fold between a 7 and a 8 , suggesting that Lys8 is the major protonation site and possibly suggesting the N-terminus as a minor charge site.
Figure Legend Snippet: Fractional abundances of the a ions from the N-terminal portion of β-lactoglobulin for a) completely oxidized, b) source activated (50V), and c) partially reduced and source activated β-lactoglobulin. The crystal structure of β-lactoglobulin is shown from two different perspectives in d) and e), with the experimental protonation sites associated with the more native structure highlighted in red and the protonation sites associated with the more unfolded structure shown in blue. Dotted spheres indicate the solvent accessibility of the protein and disulfide bonds are highlighted in yellow. *The relative abundance of fragments increased by 10-fold between a 7 and a 8 , suggesting that Lys8 is the major protonation site and possibly suggesting the N-terminus as a minor charge site.

Techniques Used:

8) Product Images from "Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin. Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin"

Article Title: Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin. Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Journal: Food Science & Nutrition

doi: 10.1002/fsn3.646

Intrinsic fluorescence emission spectra of untreated and ultrasound‐treated β‐lactoglobulin (0.005%, ω /v )
Figure Legend Snippet: Intrinsic fluorescence emission spectra of untreated and ultrasound‐treated β‐lactoglobulin (0.005%, ω /v )

Techniques Used: Fluorescence

FT ‐ IR spectrum of untreated and ultrasound‐treated β‐lactoglobulin (1%, ω /v )
Figure Legend Snippet: FT ‐ IR spectrum of untreated and ultrasound‐treated β‐lactoglobulin (1%, ω /v )

Techniques Used:

Effect of three factors on the surface hydrophobicity and free sulfhydryl group of β‐lactoglobulin
Figure Legend Snippet: Effect of three factors on the surface hydrophobicity and free sulfhydryl group of β‐lactoglobulin

Techniques Used:

Protein profiles of untreated and ultrasound‐treated β‐lactoglobulin
Figure Legend Snippet: Protein profiles of untreated and ultrasound‐treated β‐lactoglobulin

Techniques Used:

Chromatogram detection of β‐lactoglobulin samples with C 8 column (5 μm, 300 Å, 4.6 × 250 mm). Peak 1 was β‐lactoglobulin B; Peak 2 was β‐lactoglobulin A. A: β‐Lactoglobulin (standard); B: β‐lactoglobulin (untreated); C: ultrasound‐treated (20 min, AP 30%, 45°C); D: ultrasound‐treated (10 min, AP 20%, 45°C); E: ultrasound‐treated (30 min, AP 40%, 45°C); F: ultrasound‐treated (10 min, AP 40%, 45°C)
Figure Legend Snippet: Chromatogram detection of β‐lactoglobulin samples with C 8 column (5 μm, 300 Å, 4.6 × 250 mm). Peak 1 was β‐lactoglobulin B; Peak 2 was β‐lactoglobulin A. A: β‐Lactoglobulin (standard); B: β‐lactoglobulin (untreated); C: ultrasound‐treated (20 min, AP 30%, 45°C); D: ultrasound‐treated (10 min, AP 20%, 45°C); E: ultrasound‐treated (30 min, AP 40%, 45°C); F: ultrasound‐treated (10 min, AP 40%, 45°C)

Techniques Used:

The solubility of β‐lactoglobulin. A: β‐lactoglobulin (standard); B: β‐lactoglobulin (untreated); C: ultrasound‐treated (20 min, AP 30%, −45°C); D: ultrasound‐treated (10 min, AP 20%, 45°C); E: ultrasound‐treated (30 min, AP 40%, 45°C); F: ultrasound‐treated (10 min, AP 40%, 45°C)
Figure Legend Snippet: The solubility of β‐lactoglobulin. A: β‐lactoglobulin (standard); B: β‐lactoglobulin (untreated); C: ultrasound‐treated (20 min, AP 30%, −45°C); D: ultrasound‐treated (10 min, AP 20%, 45°C); E: ultrasound‐treated (30 min, AP 40%, 45°C); F: ultrasound‐treated (10 min, AP 40%, 45°C)

Techniques Used: Solubility

UV spectroscopy of untreated and ultrasound‐treated β‐lactoglobulin (0.05%, ω /v )
Figure Legend Snippet: UV spectroscopy of untreated and ultrasound‐treated β‐lactoglobulin (0.05%, ω /v )

Techniques Used: Spectroscopy

The size distribution of β‐lactoglobulin
Figure Legend Snippet: The size distribution of β‐lactoglobulin

Techniques Used:

9) Product Images from "Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS"

Article Title: Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS

Journal: International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry

doi: 10.1007/s12127-016-0201-8

Ion-neutral collisional cross section dependence on the m/z for globular proteins (myoglobin and cytochrome C) and barrel proteins (β-lactoglobulin and ubiquitin) in their native and denature states. In black, theoretical values obtained from
Figure Legend Snippet: Ion-neutral collisional cross section dependence on the m/z for globular proteins (myoglobin and cytochrome C) and barrel proteins (β-lactoglobulin and ubiquitin) in their native and denature states. In black, theoretical values obtained from

Techniques Used:

10) Product Images from "Effects of Drying Method and Excipient on Structure and Stability of Protein Solids Using Solid-State Hydrogen/Deuterium Exchange Mass Spectrometry (ssHDX-MS)"

Article Title: Effects of Drying Method and Excipient on Structure and Stability of Protein Solids Using Solid-State Hydrogen/Deuterium Exchange Mass Spectrometry (ssHDX-MS)

Journal: International journal of pharmaceutics

doi: 10.1016/j.ijpharm.2019.118470

X-ray powder diffraction powders of myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D). Samples were formulated with either sucrose (Suc), trehalose (Tre) or mannitol (Mann) and processed by either lyophilization (Lyo) or spray-drying (SD).
Figure Legend Snippet: X-ray powder diffraction powders of myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D). Samples were formulated with either sucrose (Suc), trehalose (Tre) or mannitol (Mann) and processed by either lyophilization (Lyo) or spray-drying (SD).

Techniques Used:

Solid-state FTIR spectra of formulated myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D).
Figure Legend Snippet: Solid-state FTIR spectra of formulated myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D).

Techniques Used:

Kinetics of hydrogen/deuterium exchange in the solid state for myoglobin (A), BSA (B), β-lactoglobulin (C), and lysozyme (D).
Figure Legend Snippet: Kinetics of hydrogen/deuterium exchange in the solid state for myoglobin (A), BSA (B), β-lactoglobulin (C), and lysozyme (D).

Techniques Used:

Solid-state fluorescence spectroscopy of myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D).
Figure Legend Snippet: Solid-state fluorescence spectroscopy of myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D).

Techniques Used: Fluorescence, Spectroscopy

Stability studies of formulations containing myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D).
Figure Legend Snippet: Stability studies of formulations containing myoglobin (A), BSA (B), β-lactoglobulin (C), or lysozyme (D).

Techniques Used:

Deconvoluted mass spectra of proteins pre- and post-processing for myoglobin (A), BSA (B), β-lactoglobulin (C), and lysozyme (D).
Figure Legend Snippet: Deconvoluted mass spectra of proteins pre- and post-processing for myoglobin (A), BSA (B), β-lactoglobulin (C), and lysozyme (D).

Techniques Used:

Deconvoluted mass spectra of formulations prepared by lyophilization or spray-drying with β-lactoglobulin and sucrose (A), trehalose (B), or mannitol (C).
Figure Legend Snippet: Deconvoluted mass spectra of formulations prepared by lyophilization or spray-drying with β-lactoglobulin and sucrose (A), trehalose (B), or mannitol (C).

Techniques Used:

11) Product Images from "Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins"

Article Title: Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins

Journal: Molecules

doi: 10.3390/molecules25173992

Changes in the SDS-PAGE profiles of milk proteins with 2.0 units/mL microbial transglutaminase (MTGase) at 30 °C for 0, 1, 2, or 3 h. SDS-PAGE gels were loaded using 5 μL milk samples with protein concentrations of 10 μg/well. ( A ) κ-casein (κ-CN) with MTGase; ( B ) α S -casein (α S -CN) with MTGase; ( C ) β-casein (β-CN) with MTGase; ( D ) α-lactalbumin with MTGase; ( E ) β-lactoglobulin with MTGase; and ( F ) bovine serum albumin (BSA) with MTGase; M = protein marker.
Figure Legend Snippet: Changes in the SDS-PAGE profiles of milk proteins with 2.0 units/mL microbial transglutaminase (MTGase) at 30 °C for 0, 1, 2, or 3 h. SDS-PAGE gels were loaded using 5 μL milk samples with protein concentrations of 10 μg/well. ( A ) κ-casein (κ-CN) with MTGase; ( B ) α S -casein (α S -CN) with MTGase; ( C ) β-casein (β-CN) with MTGase; ( D ) α-lactalbumin with MTGase; ( E ) β-lactoglobulin with MTGase; and ( F ) bovine serum albumin (BSA) with MTGase; M = protein marker.

Techniques Used: SDS Page, Marker

12) Product Images from "Amorphous Nanosuspensions Aggregated from Paclitaxel–Hemoglobulin Complexes with Enhanced Cytotoxicity"

Article Title: Amorphous Nanosuspensions Aggregated from Paclitaxel–Hemoglobulin Complexes with Enhanced Cytotoxicity

Journal: Pharmaceutics

doi: 10.3390/pharmaceutics10030092

Cytotoxicity of Hb and β-LG from 0.1 to 1000 μg/mL in ( A ) 4T1 and ( B ) A549 cells. Comparison of the cytotoxicity between ANSs and LPNs with the dose of PTX from 0.1 to 50 μg/mL in ( C ) 4T1 and ( D ) A549 cells. The incubation time was 48 h. ( E ) Apoptosis rate determined by flow cytometry after 48 h incubation at a PTX concentration of 10 μg/mL at 37 °C ( n = 3, ** p
Figure Legend Snippet: Cytotoxicity of Hb and β-LG from 0.1 to 1000 μg/mL in ( A ) 4T1 and ( B ) A549 cells. Comparison of the cytotoxicity between ANSs and LPNs with the dose of PTX from 0.1 to 50 μg/mL in ( C ) 4T1 and ( D ) A549 cells. The incubation time was 48 h. ( E ) Apoptosis rate determined by flow cytometry after 48 h incubation at a PTX concentration of 10 μg/mL at 37 °C ( n = 3, ** p

Techniques Used: Incubation, Flow Cytometry, Cytometry, Concentration Assay

13) Product Images from "Electrochemical Determination of β-Lactoglobulin Employing a Polystyrene Bead-Modified Carbon Nanotube Ink"

Article Title: Electrochemical Determination of β-Lactoglobulin Employing a Polystyrene Bead-Modified Carbon Nanotube Ink

Journal: Biosensors

doi: 10.3390/bios8040109

Electrochemical determination of β-lactoglobulin. Dependence of the current measured at 60 s on the β-lactoglobulin concentration at an applied potential of −0.280 V. Error bars were calculated from the standard deviation of three independent experiments. The experimental points were fitted to a power law: y = 91.2 x 0.095 , where y corresponds to the current density expressed in μA cm −2 and x to the concentration of β-lactoglobulin expressed in ppm ( R 2 = 0.977). Inset: Schematic representation of the capture immunoassay for the electrochemical determination of β-lactoglobulin (blue pentagon); Red and Ox stand for hydroquinone and 1,4 benzoquinone, respectively.
Figure Legend Snippet: Electrochemical determination of β-lactoglobulin. Dependence of the current measured at 60 s on the β-lactoglobulin concentration at an applied potential of −0.280 V. Error bars were calculated from the standard deviation of three independent experiments. The experimental points were fitted to a power law: y = 91.2 x 0.095 , where y corresponds to the current density expressed in μA cm −2 and x to the concentration of β-lactoglobulin expressed in ppm ( R 2 = 0.977). Inset: Schematic representation of the capture immunoassay for the electrochemical determination of β-lactoglobulin (blue pentagon); Red and Ox stand for hydroquinone and 1,4 benzoquinone, respectively.

Techniques Used: Concentration Assay, Standard Deviation

14) Product Images from "Allergen-responsive CD4+CD25+ Regulatory T Cells in Children who Have Outgrown Cow's Milk Allergy"

Article Title: Allergen-responsive CD4+CD25+ Regulatory T Cells in Children who Have Outgrown Cow's Milk Allergy

Journal: The Journal of Experimental Medicine

doi: 10.1084/jem.20032121

Proliferation of PBMCs. (A) PBMCs were purified from samples obtained before and 1 wk after in vivo challenge with cow's milk and then stimulated in vitro with bovine β-LG. Radioactive thymidine ( 3 H-Tdr) was added 6 d after addition of β-LG to the PBMC cultures. The cells were harvested 12–16 h later. Incorporation of 3 H-Tdr was determined in a β-counter. •, children with active allergy; ○, tolerant children (outgrown allergy). (B) Similar samples and procedure as in A, but stimulation was performed with PHA. Student's t test was used for statistical analysis.
Figure Legend Snippet: Proliferation of PBMCs. (A) PBMCs were purified from samples obtained before and 1 wk after in vivo challenge with cow's milk and then stimulated in vitro with bovine β-LG. Radioactive thymidine ( 3 H-Tdr) was added 6 d after addition of β-LG to the PBMC cultures. The cells were harvested 12–16 h later. Incorporation of 3 H-Tdr was determined in a β-counter. •, children with active allergy; ○, tolerant children (outgrown allergy). (B) Similar samples and procedure as in A, but stimulation was performed with PHA. Student's t test was used for statistical analysis.

Techniques Used: Purification, In Vivo, In Vitro

Fold increase or decrease in proliferation after depletion of CD25 + cells from PBMCs purified from blood before and 1 wk after in vivo challenge with cow's milk. Predepletion level (see Fig. 3 A) is set to 1 (dotted line). The depleted and nondepleted PBMC samples were tested for proliferative activity, unstimulated and after in vitro stimulation with bovine β-LG or the mitogen PHA. Radioactive thymidine ( 3 H-Tdr) was added 6 d after addition of antigens to the cell cultures. The cells were harvested 12–16 h later. Incorporation of 3 H-Tdr was determined in a β-counter. Student's t test was used for statistical analysis. For comparison with absolute proliferative activity (cpm values) of in vitro–stimulated PBMCs collected from allergic and tolerant children before and after in vivo challenge, see Fig 3 A.
Figure Legend Snippet: Fold increase or decrease in proliferation after depletion of CD25 + cells from PBMCs purified from blood before and 1 wk after in vivo challenge with cow's milk. Predepletion level (see Fig. 3 A) is set to 1 (dotted line). The depleted and nondepleted PBMC samples were tested for proliferative activity, unstimulated and after in vitro stimulation with bovine β-LG or the mitogen PHA. Radioactive thymidine ( 3 H-Tdr) was added 6 d after addition of antigens to the cell cultures. The cells were harvested 12–16 h later. Incorporation of 3 H-Tdr was determined in a β-counter. Student's t test was used for statistical analysis. For comparison with absolute proliferative activity (cpm values) of in vitro–stimulated PBMCs collected from allergic and tolerant children before and after in vivo challenge, see Fig 3 A.

Techniques Used: Purification, In Vivo, Activity Assay, In Vitro

Generation of the immunosuppressive cytokines TGF-β1-LAP and IL-10 by PBMCs purified from blood of allergic or tolerant children before and 1 wk after in vivo challenge with cow's milk. (A) Production of TGF-β1-LAP determined in supernatants from PBMCs stimulated for 96 h with β-LG (1 mg/ml) or PHA (50 μg/ml) by subtracting the TGF-β1-LAP concentration in unstimulated wells. (B) Production of IL-10 under the same culture conditions as in A. Student's t test was used for statistical analysis.
Figure Legend Snippet: Generation of the immunosuppressive cytokines TGF-β1-LAP and IL-10 by PBMCs purified from blood of allergic or tolerant children before and 1 wk after in vivo challenge with cow's milk. (A) Production of TGF-β1-LAP determined in supernatants from PBMCs stimulated for 96 h with β-LG (1 mg/ml) or PHA (50 μg/ml) by subtracting the TGF-β1-LAP concentration in unstimulated wells. (B) Production of IL-10 under the same culture conditions as in A. Student's t test was used for statistical analysis.

Techniques Used: Purification, In Vivo, Concentration Assay

15) Product Images from "Effects of the Oral Administration of Viable and Heat-Killed Streptococcus bovis HC5 Cells to Pre-Sensitized BALB/c Mice"

Article Title: Effects of the Oral Administration of Viable and Heat-Killed Streptococcus bovis HC5 Cells to Pre-Sensitized BALB/c Mice

Journal: PLoS ONE

doi: 10.1371/journal.pone.0048313

β-lactoglobulin levels in animal sera from the treatment groups. An intragastrically dose of β-LG (20 mg) was administered as a bystander protein to the negative control group and the groups that received S. bovis HC5 (viable and heat-killed cells). At the indicated time points following β-LG administration, the levels of β-LG in mice sera were determined by FPLC. The results show an average of the β-LG level detected in a pool of animal's sera from each group. β-LG was not detected in all serum samples from negative control group. (NC) negative control group; (V) mice treated with viable S. bovis HC5 cells; (HK) mice treated with heat-killed S. bovis HC5 cells (HK).
Figure Legend Snippet: β-lactoglobulin levels in animal sera from the treatment groups. An intragastrically dose of β-LG (20 mg) was administered as a bystander protein to the negative control group and the groups that received S. bovis HC5 (viable and heat-killed cells). At the indicated time points following β-LG administration, the levels of β-LG in mice sera were determined by FPLC. The results show an average of the β-LG level detected in a pool of animal's sera from each group. β-LG was not detected in all serum samples from negative control group. (NC) negative control group; (V) mice treated with viable S. bovis HC5 cells; (HK) mice treated with heat-killed S. bovis HC5 cells (HK).

Techniques Used: Negative Control, Mouse Assay, Fast Protein Liquid Chromatography

16) Product Images from "Low-Frequency Modes of Peptides and Globular Proteins in Solution Observed by Ultrafast OHD-RIKES Spectroscopy"

Article Title: Low-Frequency Modes of Peptides and Globular Proteins in Solution Observed by Ultrafast OHD-RIKES Spectroscopy

Journal: Biophysical Journal

doi:

Raw OHD-RIKES spectra of the four globular proteins lysozyme,  α -lactalbumin,  β -lactoglobulin, and pepsin in aqueous solution, along with the spectrum of water scaled in proportion to the sample water content.
Figure Legend Snippet: Raw OHD-RIKES spectra of the four globular proteins lysozyme, α -lactalbumin, β -lactoglobulin, and pepsin in aqueous solution, along with the spectrum of water scaled in proportion to the sample water content.

Techniques Used:

17) Product Images from "Mass Spectrometric Immunoassay for Quantitative Determination of Transthyretin and its Variants"

Article Title: Mass Spectrometric Immunoassay for Quantitative Determination of Transthyretin and its Variants

Journal: Proteomics

doi: 10.1002/pmic.201100023

(a) Representative transthyretin standards mass spectra, and (b) Standard curve generated with the transthyretin (TTR) mass spectrometric immunoassay by using beta-lactoglobulin (BL) as an internal reference standard.
Figure Legend Snippet: (a) Representative transthyretin standards mass spectra, and (b) Standard curve generated with the transthyretin (TTR) mass spectrometric immunoassay by using beta-lactoglobulin (BL) as an internal reference standard.

Techniques Used: Generated

18) Product Images from "Characterization of protein adsorption onto silica nanoparticles: influence of pH and ionic strength"

Article Title: Characterization of protein adsorption onto silica nanoparticles: influence of pH and ionic strength

Journal: Colloid and Polymer Science

doi: 10.1007/s00396-015-3754-x

Adsorption isotherms of ß-lactoglobulin on Ludox TMA for several pH values without added salt: a pH ≤ pH 4; b pH ≥ pH 4. Experimental data ( symbols ) and fits by the GAB model ( lines ). The monolayer capacity based on a dense packing of monomeric protein ( A 0 = 13 nm 2 ) is indicated by the dashed line ; see also caption of Fig. 2
Figure Legend Snippet: Adsorption isotherms of ß-lactoglobulin on Ludox TMA for several pH values without added salt: a pH ≤ pH 4; b pH ≥ pH 4. Experimental data ( symbols ) and fits by the GAB model ( lines ). The monolayer capacity based on a dense packing of monomeric protein ( A 0 = 13 nm 2 ) is indicated by the dashed line ; see also caption of Fig. 2

Techniques Used: Adsorption

ß-Lactoglobulin adsorption: Fit values of the GAB parameters as a function of pH for three ionic strengths (no salt, 25 mM, 100 mM NaCl): a limiting surface concentration Γ m of strongly bound protein; b adsorption constant K S ; c adsorption constant K L ; d adsorption ratio Γ ( c * )/ Γ m for c * = 2 mg/mL (see text)
Figure Legend Snippet: ß-Lactoglobulin adsorption: Fit values of the GAB parameters as a function of pH for three ionic strengths (no salt, 25 mM, 100 mM NaCl): a limiting surface concentration Γ m of strongly bound protein; b adsorption constant K S ; c adsorption constant K L ; d adsorption ratio Γ ( c * )/ Γ m for c * = 2 mg/mL (see text)

Techniques Used: Adsorption, Concentration Assay

Comparison of lysozyme and ß-lactoglobulin adsorption onto silica nanoparticles: Adsorbed amount Γ ( c * ) at the reference concentration c * = 2 mg/mL plotted against pH: filled square , no salt; filled circle , 25 mM NaCl; filled triangle , 100 mM NaCl. The isoelectric points (pI) of the proteins are indicated by vertical dashed lines
Figure Legend Snippet: Comparison of lysozyme and ß-lactoglobulin adsorption onto silica nanoparticles: Adsorbed amount Γ ( c * ) at the reference concentration c * = 2 mg/mL plotted against pH: filled square , no salt; filled circle , 25 mM NaCl; filled triangle , 100 mM NaCl. The isoelectric points (pI) of the proteins are indicated by vertical dashed lines

Techniques Used: Adsorption, Concentration Assay

Adsorption isotherms of ß-lactoglobulin on Ludox TMA at a pH 4; b pH 5; c pH 6; d pH 7. Experimental data: filled square , no salt; filled circle , 25 mM NaCl; filled triangle , 100 mM NaCl; full lines : fit by the GAB equation. The estimated monolayer capacity is indicated by a dashed line . See caption to Fig. 2 for further details
Figure Legend Snippet: Adsorption isotherms of ß-lactoglobulin on Ludox TMA at a pH 4; b pH 5; c pH 6; d pH 7. Experimental data: filled square , no salt; filled circle , 25 mM NaCl; filled triangle , 100 mM NaCl; full lines : fit by the GAB equation. The estimated monolayer capacity is indicated by a dashed line . See caption to Fig. 2 for further details

Techniques Used: Adsorption

a Zeta potential of Ludox TMA silica particles as a function of pH for two different ionic strengths (see Table 2 ). b Estimated net charge of lysozyme and ß-lactoglobulin as a function of pH
Figure Legend Snippet: a Zeta potential of Ludox TMA silica particles as a function of pH for two different ionic strengths (see Table 2 ). b Estimated net charge of lysozyme and ß-lactoglobulin as a function of pH

Techniques Used:

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    Millipore β lg
    Mice treated with anti-CD4 are competent to respond to unrelated antigens. (A) Mice initially tolerized to OVA or <t>β-LG</t> (as described in previous figures) were sensitized i.p. with a different antigen at days 50 and 64, and challenged i.n. with the same antigen used at day 50. (B) Only animals tolerized to the same antigen used for sensitization at day 50 were protected from BAL eosinophilia (n = 6, *** P
    β Lg, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Price from $9.99 to $1999.99
    β lg - by Bioz Stars, 2022-10
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    93
    Millipore β lactoglobulin
    ( A – E ) AFM images of ( A ) multilamellar DMPG lipid bilayers, ( B ) multilamellar DMPG lipid bilayers, and adsorbed  β LG; ( C ) multilamellar DMPC lipid bilayers, ( D ) multilamellar DMPC lipid bilayers, and adsorbed  β LG; and ( E )  β LG adsorbed on to a Ge IRE surface. All images are shown on the same vertical scale for comparison purposes. ( F – J ) Simultaneously acquired ATR-FTIR spectra shown beside their corresponding AFM images. Scale bar: 0.2 absorbance units.
    β Lactoglobulin, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β lactoglobulin/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    β lactoglobulin - by Bioz Stars, 2022-10
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    Mice treated with anti-CD4 are competent to respond to unrelated antigens. (A) Mice initially tolerized to OVA or β-LG (as described in previous figures) were sensitized i.p. with a different antigen at days 50 and 64, and challenged i.n. with the same antigen used at day 50. (B) Only animals tolerized to the same antigen used for sensitization at day 50 were protected from BAL eosinophilia (n = 6, *** P

    Journal: PLoS ONE

    Article Title: Prevention of House Dust Mite Induced Allergic Airways Disease in Mice through Immune Tolerance

    doi: 10.1371/journal.pone.0022320

    Figure Lengend Snippet: Mice treated with anti-CD4 are competent to respond to unrelated antigens. (A) Mice initially tolerized to OVA or β-LG (as described in previous figures) were sensitized i.p. with a different antigen at days 50 and 64, and challenged i.n. with the same antigen used at day 50. (B) Only animals tolerized to the same antigen used for sensitization at day 50 were protected from BAL eosinophilia (n = 6, *** P

    Article Snippet: Animals were sensitized, at the times described in the text, by i.p. injection of 20 µg in 2.0 mg of endotoxin-free aluminum hydroxide (Alu-gel-S, Serva, Heidelberg, Germany) of OVA or β-LG (Sigma, St Louis, USA) previously run through a DetoxyGel column (Pierce, Rockford, USA), or HDM extract (Greer, Lenoir, USA).

    Techniques: Mouse Assay

    Tolerogenic effect of anti-CD4 treatment is antigen-specific and effective in sensitized animals. (A) BALB/c mice sensitized with OVA-alum or HDM-alum were tolerized to the same antigens on days 50 and 64, and challenged i.n. with the same antigens. (B) Sensitized mice subsequently treated with OVA or HDM under the cover of anti-CD4 showed protection from AHR (n = 8 for OVA, n = 6 to HDM). Data are representative of two independent experiments. (C) Mice were initially sensitized with OVA-alum or β-LG-alum, and tolerized to the same or a different antigen on days 50 and 64. All mice were challenged i.n. with the same antigen used for initial sensitization. (D) Mice treated with a different antigen together with anti-CD4 did not show reduced BAL eosinophilia (OVA > tβ-LG and β-LG > tOVA) while treatment with anti-CD4 and the same antigen used for sensitization showed a significant reduction of BAL eosinophilia (OVA > tOVA and β-LG > tβ-LG; n = 6, *** P

    Journal: PLoS ONE

    Article Title: Prevention of House Dust Mite Induced Allergic Airways Disease in Mice through Immune Tolerance

    doi: 10.1371/journal.pone.0022320

    Figure Lengend Snippet: Tolerogenic effect of anti-CD4 treatment is antigen-specific and effective in sensitized animals. (A) BALB/c mice sensitized with OVA-alum or HDM-alum were tolerized to the same antigens on days 50 and 64, and challenged i.n. with the same antigens. (B) Sensitized mice subsequently treated with OVA or HDM under the cover of anti-CD4 showed protection from AHR (n = 8 for OVA, n = 6 to HDM). Data are representative of two independent experiments. (C) Mice were initially sensitized with OVA-alum or β-LG-alum, and tolerized to the same or a different antigen on days 50 and 64. All mice were challenged i.n. with the same antigen used for initial sensitization. (D) Mice treated with a different antigen together with anti-CD4 did not show reduced BAL eosinophilia (OVA > tβ-LG and β-LG > tOVA) while treatment with anti-CD4 and the same antigen used for sensitization showed a significant reduction of BAL eosinophilia (OVA > tOVA and β-LG > tβ-LG; n = 6, *** P

    Article Snippet: Animals were sensitized, at the times described in the text, by i.p. injection of 20 µg in 2.0 mg of endotoxin-free aluminum hydroxide (Alu-gel-S, Serva, Heidelberg, Germany) of OVA or β-LG (Sigma, St Louis, USA) previously run through a DetoxyGel column (Pierce, Rockford, USA), or HDM extract (Greer, Lenoir, USA).

    Techniques: Mouse Assay

    TPE-MI preferentially reacts with buried cysteine thiols in unfolded proteins and switches on fluorescence. Shown are representative reaction kinetics for four proteins (note that the absolute fluorescence values between graphs here and in other figures cannot be compared to each other due to differences in instrument settings). a Bovine β-lactoglobulin, which contains five thiols: one buried free thiol and four disulphide-linked thiols; and bovine ubiquitin, which contains no thiols. b Saccharomyces cerevisiae enolase, which contains one buried free thiol and c human peroxiredoxin 3, which contains three thiols: one buried free thiol and two disulphide-linked surface-exposed thiols. Proteins were suspended in 100 mM sodium phosphate, pH 7.4, alone or supplemented with guandine hydrochloride (GuHCl) to induce denaturation. At the start of the reaction 50 μM TPE-MI was added. d Same design but with 50 μM N -methylmaleimide (NMM) added before the addition of TPE-MI.

    Journal: Nature Communications

    Article Title: A thiol probe for measuring unfolded protein load and proteostasis in cells

    doi: 10.1038/s41467-017-00203-5

    Figure Lengend Snippet: TPE-MI preferentially reacts with buried cysteine thiols in unfolded proteins and switches on fluorescence. Shown are representative reaction kinetics for four proteins (note that the absolute fluorescence values between graphs here and in other figures cannot be compared to each other due to differences in instrument settings). a Bovine β-lactoglobulin, which contains five thiols: one buried free thiol and four disulphide-linked thiols; and bovine ubiquitin, which contains no thiols. b Saccharomyces cerevisiae enolase, which contains one buried free thiol and c human peroxiredoxin 3, which contains three thiols: one buried free thiol and two disulphide-linked surface-exposed thiols. Proteins were suspended in 100 mM sodium phosphate, pH 7.4, alone or supplemented with guandine hydrochloride (GuHCl) to induce denaturation. At the start of the reaction 50 μM TPE-MI was added. d Same design but with 50 μM N -methylmaleimide (NMM) added before the addition of TPE-MI.

    Article Snippet: Maleic anhydride, sodium acetate, sodium carbonate, glutathione (GSH), guanidine hydrochloride (GuHCl), bovine β-lactoglobulin, yeast (Saccharomyces cerevisiae ) enolase, bovine ubiquitin, NMM, tunicamycin and other reagents were purchased from Sigma-Aldrich and used as received.

    Techniques: Fluorescence

    TPE-MI fluorescence is not activated by glutathione reaction and can detect increases in unfolded protein load in cell lysates. a Reactivity of TPE-MI (50 μM) with β-lactoglobulin (250 μM) in the presence of the small thiol containing peptide glutathione (0.025 mM–8 mM GSH) and 4.6 M GuHCl. Fluorescence intensity of TPE-MI with different concentrations of GSH is shown for comparison (measured in 4.6 M GuHCl). Arrow indicates 7:3 protein thiol to glutathione thiol ratio found intracellularly. b Reaction kinetics of 50 µM TPE-MI in the presence of intact and unfolded cell lysates from mouse Neuro2a neuroblastoma cells (0.5 mg ml −1 total cellular protein). Shown are ‘native’ cell lysate in 100 mM sodium phosphate, pH 7.4 and ‘unfolded’ cell lysate containing 4.6 M GuHCl.

    Journal: Nature Communications

    Article Title: A thiol probe for measuring unfolded protein load and proteostasis in cells

    doi: 10.1038/s41467-017-00203-5

    Figure Lengend Snippet: TPE-MI fluorescence is not activated by glutathione reaction and can detect increases in unfolded protein load in cell lysates. a Reactivity of TPE-MI (50 μM) with β-lactoglobulin (250 μM) in the presence of the small thiol containing peptide glutathione (0.025 mM–8 mM GSH) and 4.6 M GuHCl. Fluorescence intensity of TPE-MI with different concentrations of GSH is shown for comparison (measured in 4.6 M GuHCl). Arrow indicates 7:3 protein thiol to glutathione thiol ratio found intracellularly. b Reaction kinetics of 50 µM TPE-MI in the presence of intact and unfolded cell lysates from mouse Neuro2a neuroblastoma cells (0.5 mg ml −1 total cellular protein). Shown are ‘native’ cell lysate in 100 mM sodium phosphate, pH 7.4 and ‘unfolded’ cell lysate containing 4.6 M GuHCl.

    Article Snippet: Maleic anhydride, sodium acetate, sodium carbonate, glutathione (GSH), guanidine hydrochloride (GuHCl), bovine β-lactoglobulin, yeast (Saccharomyces cerevisiae ) enolase, bovine ubiquitin, NMM, tunicamycin and other reagents were purchased from Sigma-Aldrich and used as received.

    Techniques: Fluorescence

    Effect of emulsifier types on emulsification at 60 °C with microchannel plate type A (MC-A, see Section 3.2 .) using ( a ) sodium dodecyl sulfate (SDS), ( b ) hexaglycerin monolaulate (HGML), ( c,d ) Tween 80, ( e ) sodium caseinate (SC), ( f ) β-lactoglobulin (β-LG), and ( g ) skimmed milk powder. The concentration of each emulsifier was 3 wt%.

    Journal: Molecules

    Article Title: Protein-Stabilized Palm-Oil-in-Water Emulsification Using Microchannel Array Devices under Controlled Temperature

    doi: 10.3390/molecules25204805

    Figure Lengend Snippet: Effect of emulsifier types on emulsification at 60 °C with microchannel plate type A (MC-A, see Section 3.2 .) using ( a ) sodium dodecyl sulfate (SDS), ( b ) hexaglycerin monolaulate (HGML), ( c,d ) Tween 80, ( e ) sodium caseinate (SC), ( f ) β-lactoglobulin (β-LG), and ( g ) skimmed milk powder. The concentration of each emulsifier was 3 wt%.

    Article Snippet: ChemicalsPalm oil (refined, analytical standard grade), β-lactoglobulin (β-LG) from bovine milk (≧85%, lyophilized powder), and calcein were purchased from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques: Concentration Assay

    ( A – E ) AFM images of ( A ) multilamellar DMPG lipid bilayers, ( B ) multilamellar DMPG lipid bilayers, and adsorbed  β LG; ( C ) multilamellar DMPC lipid bilayers, ( D ) multilamellar DMPC lipid bilayers, and adsorbed  β LG; and ( E )  β LG adsorbed on to a Ge IRE surface. All images are shown on the same vertical scale for comparison purposes. ( F – J ) Simultaneously acquired ATR-FTIR spectra shown beside their corresponding AFM images. Scale bar: 0.2 absorbance units.

    Journal: Biophysical Journal

    Article Title: Tracking Molecular Interactions in Membranes by Simultaneous ATR-FTIR-AFM

    doi: 10.1016/j.bpj.2009.06.013

    Figure Lengend Snippet: ( A – E ) AFM images of ( A ) multilamellar DMPG lipid bilayers, ( B ) multilamellar DMPG lipid bilayers, and adsorbed β LG; ( C ) multilamellar DMPC lipid bilayers, ( D ) multilamellar DMPC lipid bilayers, and adsorbed β LG; and ( E ) β LG adsorbed on to a Ge IRE surface. All images are shown on the same vertical scale for comparison purposes. ( F – J ) Simultaneously acquired ATR-FTIR spectra shown beside their corresponding AFM images. Scale bar: 0.2 absorbance units.

    Article Snippet: All buffer materials and β -lactoglobulin ( β LG) were purchased from Sigma-Aldrich and used without further purification.

    Techniques: