chromatographies  (GE Healthcare)

 
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    Grade 4 Chr Cellulose Chromatography Paper roll ×
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    Structured Review

    GE Healthcare chromatographies
    MALDI-TOF analysis of a rhGCase sample purified by HIC and IEC <t>chromatography.</t> Red bars indicate rhGCase tryptic peptides assigned to human GCase regions. The position of the five putative N-glycosylation sites is shown by circles; all sites except the last one, which never harbours glycans (Berg-Fussman et al. 1993 ), are normally occupied by oligosaccharidic chains.

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    Images

    1) Product Images from "Endosperm-specific expression of human acid beta-glucosidase in a waxy rice"

    Article Title: Endosperm-specific expression of human acid beta-glucosidase in a waxy rice

    Journal: Rice

    doi: 10.1186/1939-8433-5-34

    MALDI-TOF analysis of a rhGCase sample purified by HIC and IEC chromatography. Red bars indicate rhGCase tryptic peptides assigned to human GCase regions. The position of the five putative N-glycosylation sites is shown by circles; all sites except the last one, which never harbours glycans (Berg-Fussman et al. 1993 ), are normally occupied by oligosaccharidic chains.
    Figure Legend Snippet: MALDI-TOF analysis of a rhGCase sample purified by HIC and IEC chromatography. Red bars indicate rhGCase tryptic peptides assigned to human GCase regions. The position of the five putative N-glycosylation sites is shown by circles; all sites except the last one, which never harbours glycans (Berg-Fussman et al. 1993 ), are normally occupied by oligosaccharidic chains.

    Techniques Used: Purification, Hydrophobic Interaction Chromatography, Chromatography

    SDS-PAGE analysis carried out to estimate contaminant removal obtained in each chromatographic step. Lane 1: HIC (Hydrophobic Interaction Chromatography) eluate; 2: IEC (Ion Exchange Chromatography) eluate; 3: GF (Gel Filtration) eluate.
    Figure Legend Snippet: SDS-PAGE analysis carried out to estimate contaminant removal obtained in each chromatographic step. Lane 1: HIC (Hydrophobic Interaction Chromatography) eluate; 2: IEC (Ion Exchange Chromatography) eluate; 3: GF (Gel Filtration) eluate.

    Techniques Used: SDS Page, Hydrophobic Interaction Chromatography, Ion Exchange Chromatography, Filtration

    Related Articles

    Generated:

    Article Title: Metabolomics reveals metabolic changes in male reproductive cells exposed to thirdhand smoke
    Article Snippet: Cell culture and THS treatment Smoke samples were generated in a laboratory system to simulate chronic THS pollution, as described previously . .. Briefly, the chronic THS samples were generated by exposing chromatography paper (3 MM Chr, Whatman, GE Lifesciences, Pittsburgh, PA, USA) to cigarette smoke in a 6 m3 stainless steel chamber for a total of 32 h over 20 days, with a total smoke exposure of 545 mg particulate material. ..

    Chromatography:

    Article Title: Metabolomics reveals metabolic changes in male reproductive cells exposed to thirdhand smoke
    Article Snippet: Cell culture and THS treatment Smoke samples were generated in a laboratory system to simulate chronic THS pollution, as described previously . .. Briefly, the chronic THS samples were generated by exposing chromatography paper (3 MM Chr, Whatman, GE Lifesciences, Pittsburgh, PA, USA) to cigarette smoke in a 6 m3 stainless steel chamber for a total of 32 h over 20 days, with a total smoke exposure of 545 mg particulate material. ..

    Article Title: Resonance Energy Transfer-Based Biosensors for Point-of-Need Diagnosis—Progress and Perspectives
    Article Snippet: .. Filter or chromatography paper by Whatman are commonly used for paper-based assays. ..

    Article Title: YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3?
    Article Snippet: Reagents and antibodies Reagents were obtained from Sigma-Aldrich unless specified otherwise. .. Chromatography reagents and γ-[32 P]ATP (3,000 Ci/mmol and 10 mCi/ml) were obtained from Amersham Biosciences. .. Antisera specific to YSK1 was raised in rabbits 4256 and 4257 immunized with recombinant human YSK1 by Biogenes, and then affinity purified over a column of YSK1 coupled to Affigel-15 (Bio-Rad Laboratories).

    Article Title: Volatile allosteric antagonists of mosquito odorant receptors inhibit normal odor-dependent behaviors
    Article Snippet: .. Tested compounds were applied on chromatography paper (Whatman), over a 24 cm2 total area, at three doses equivalent to 0.2, 0.04 and 0.01 μL/cm2 (1000-1400, 200-280 and 50-70 nmole/cm2 , respectively, depending on compound molecular mass; see also ) diluted with dichloromethane (DCM). .. Tested compounds were applied on chromatography paper (Whatman), over a 24 cm2 total area, at three doses equivalent to 0.2, 0.04 and 0.01 μL/cm2 (1000-1400, 200-280 and 50-70 nmole/cm2 , respectively, depending on compound molecular mass; see also ) diluted with dichloromethane (DCM).

    Article Title: A Novel One-Step Fabricated, Droplet-Based Electrochemical Sensor for Facile Biochemical Assays
    Article Snippet: As discussed later, the proposed EC sensor has been used for the determination of dGTP, which is usually an indispensable reaction substrate for PCR-based DNA amplification. .. It is necessary to state that when Whatman #1 chromatography paper, office paper, or polypropylene paper was used as the substrate material, the formation of the droplet on the fabricated sensor was not successful. .. For chromatography paper and office paper, the solution spread quickly in the horizontal direction, while in the vertical direction the solution permeated into the paper substrate.

    Article Title: The Initial Response of a Eukaryotic Replisome to DNA Damage
    Article Snippet: .. Denaturing gels were fixed with two changes of cold 5% trichloroacetic acid and dried onto chromatography paper (Whatman). .. Native gels were dried directly onto chromatography paper.

    Article Title: Artemisinin permeability via Caco-2 cells increases after simulated digestion of Artemisia annua leaves
    Article Snippet: .. Digestions were run through oral, gastric, and intestinal stages of digestion and then filtered through Whatman #1 chromatography paper (0.16 mm thickness, porosity < 10 μm) to separate liquid and solid fractions. .. Only the liquid fraction of the digestate was used for permeability experiments.

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    GE Healthcare protein a sepharose affinity chromatography
    Purification of dimeric and monomeric human ephrin-A5. The protein was expressed as an Fc fusion in HEK293 cells and was purified from culture supernatant by <t>Protein-A</t> <t>Sepharose</t> affinity chromatography (lane 1 ) and Superdex-200 size exclusion chromatography
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    GE Healthcare fast protein liquid chromatography fplc
    T12, a peptidomimetic of the GPBP region comprising 260 SHCIE 264 motif disturbs multimerization ( A ) Chemical structure of T12 and dose-response effects on GPBP autophosphorylation and A549 doxorubicin IC50. Phosphorylation mixtures were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), blotted and exposed ( 32 P) prior to detect GPBP with N27 (WB). Specific activities (histogram) were calculated using WCIF ImageJ and represented as percentage (mean ± standard error of the mean, SEM) of control mixture (−) that was set at 100%. Statistics: 1WA and Fisher’s (1WA-F), n = 2. Graph and Table show the efficacy and IC50 of doxorubicin on A549 cultures at the indicated T12 concentrations. Efficacy values are mean ± SD. The 2WA and Tukey’s (2WA-T) and IC50 are indicated, n = 4. Representative of five assays. ( B ) Recombinant (multimer or trimer, n = 3) or extracellular native (A427, n = 2) GPBP were analyzed as in A at 50 µM T12. Statistics: Student’s t -test. ( C ) Similar amounts (125 μg) of recombinant extracellular GPBP and bovine serum albumin (BSA) were exposed to T12 (10 mM) during 15 min at room temperature and further <t>FPLC-SEC</t> analyzed essentially as in previous Figure. Represented is one out of three independent analysis performed from two different GPBP preparations.
    Fast Protein Liquid Chromatography Fplc, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione affinity chromatography glutathione affinity chromatography
    (A) Two-dimensional gel electropherogram of <t>glutathione</t> <t>affinity</t> <t>chromatography</t> fractions possessing GST activity. (B) Enlarged image of the boxed region showing grouping based on mass spectrometry fingerprints (refer to Table 1 ). IEF strip pI3-10NL was rehydrated in the protein precipitate from GST active fractions of the GSTrap column. This was focused for 48 kVh and then separated on a 10% polyacrylamide gel and stained with SYPRO Ruby.
    Glutathione Affinity Chromatography Glutathione Affinity Chromatography, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    GE Healthcare heparin sepharose chromatography
    Analytical <t>heparin-Sepharose</t> column elution profiles for thrombin, α 1 AT pitts , and their complex. A , elution profile of proteins and complexes, as indicated. It can be seen that α 1 AT pitts , native or cleaved ( peaks 1 and 4 ), does not bind
    Heparin Sepharose Chromatography, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Purification of dimeric and monomeric human ephrin-A5. The protein was expressed as an Fc fusion in HEK293 cells and was purified from culture supernatant by Protein-A Sepharose affinity chromatography (lane 1 ) and Superdex-200 size exclusion chromatography

    Journal:

    Article Title: Kinetic analysis of the binding of monomeric and dimeric ephrins to Eph receptors: Correlation to function in a growth cone collapse assay

    doi: 10.1110/ps.062608807

    Figure Lengend Snippet: Purification of dimeric and monomeric human ephrin-A5. The protein was expressed as an Fc fusion in HEK293 cells and was purified from culture supernatant by Protein-A Sepharose affinity chromatography (lane 1 ) and Superdex-200 size exclusion chromatography

    Article Snippet: The proteins were purified from cell culture supernatants (DMEM, 10% fetal bovine serum, 20 mg/mL penicillin-streptomycin [Gibco]) by Protein-A Sepharose affinity chromatography (Amersham Biosciences).

    Techniques: Purification, Affinity Chromatography, Size-exclusion Chromatography

    T12, a peptidomimetic of the GPBP region comprising 260 SHCIE 264 motif disturbs multimerization ( A ) Chemical structure of T12 and dose-response effects on GPBP autophosphorylation and A549 doxorubicin IC50. Phosphorylation mixtures were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), blotted and exposed ( 32 P) prior to detect GPBP with N27 (WB). Specific activities (histogram) were calculated using WCIF ImageJ and represented as percentage (mean ± standard error of the mean, SEM) of control mixture (−) that was set at 100%. Statistics: 1WA and Fisher’s (1WA-F), n = 2. Graph and Table show the efficacy and IC50 of doxorubicin on A549 cultures at the indicated T12 concentrations. Efficacy values are mean ± SD. The 2WA and Tukey’s (2WA-T) and IC50 are indicated, n = 4. Representative of five assays. ( B ) Recombinant (multimer or trimer, n = 3) or extracellular native (A427, n = 2) GPBP were analyzed as in A at 50 µM T12. Statistics: Student’s t -test. ( C ) Similar amounts (125 μg) of recombinant extracellular GPBP and bovine serum albumin (BSA) were exposed to T12 (10 mM) during 15 min at room temperature and further FPLC-SEC analyzed essentially as in previous Figure. Represented is one out of three independent analysis performed from two different GPBP preparations.

    Journal: Oncotarget

    Article Title: Selective targeting of collagen IV in the cancer cell microenvironment reduces tumor burden

    doi: 10.18632/oncotarget.24280

    Figure Lengend Snippet: T12, a peptidomimetic of the GPBP region comprising 260 SHCIE 264 motif disturbs multimerization ( A ) Chemical structure of T12 and dose-response effects on GPBP autophosphorylation and A549 doxorubicin IC50. Phosphorylation mixtures were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), blotted and exposed ( 32 P) prior to detect GPBP with N27 (WB). Specific activities (histogram) were calculated using WCIF ImageJ and represented as percentage (mean ± standard error of the mean, SEM) of control mixture (−) that was set at 100%. Statistics: 1WA and Fisher’s (1WA-F), n = 2. Graph and Table show the efficacy and IC50 of doxorubicin on A549 cultures at the indicated T12 concentrations. Efficacy values are mean ± SD. The 2WA and Tukey’s (2WA-T) and IC50 are indicated, n = 4. Representative of five assays. ( B ) Recombinant (multimer or trimer, n = 3) or extracellular native (A427, n = 2) GPBP were analyzed as in A at 50 µM T12. Statistics: Student’s t -test. ( C ) Similar amounts (125 μg) of recombinant extracellular GPBP and bovine serum albumin (BSA) were exposed to T12 (10 mM) during 15 min at room temperature and further FPLC-SEC analyzed essentially as in previous Figure. Represented is one out of three independent analysis performed from two different GPBP preparations.

    Article Snippet: Fast protein liquid chromatography (FPLC)-SEC were performed using a Superdex 200 column (GE Healthcare) and high-performance liquid chromatography (HPLC)-SEC using a TSKgel® G4000SW column (Sigma-Aldrich).

    Techniques: Polyacrylamide Gel Electrophoresis, SDS Page, Western Blot, Recombinant, Fast Protein Liquid Chromatography, Size-exclusion Chromatography

    The druggable GPBP isoform is a multimer stabilized by self-interacting 260 SHCIE 264 motif ( A ) The indicated recombinant GPBP pools were analyzed by fast protein liquid chromatography (FPLC)-SEC. Calibrators, MW (kDa) and elution volumes (mL) were: thyroglobulin (669, 6.86), aldolase (158, 12.35) and serum human albumin (66, 13.89). In all chromatograms, the positions of the main GPBP oligomers are denoted. ( B ) Media (2.5 L) from the indicated cultures were affinity-purified using single-chain variable fragment (scFv)N26-column. Bound material was eluted in native conditions using N26-competing synthetic peptide (PS132) and analyzed as in A. Represented in AU are the FI of individual fractions in indirect ELISA analysis using anti-GPBP monoclonal antibodies (mAb). Shown is a representative assay of three. Image , mAb N27-developed WB of similarly purified (25 mL) GPBP eluted under denaturing conditions. Numbers and bars here and in following WB denote kDa and position of MW markers, respectively. ( C ) Structural features such as PH (empty box) and Start (scratched box) domains are indicated and represent GPBP and deletion mutants thereof. Indicated are spanning residues (numbers) and YTH interaction using colony-lift filter assays (+ or −). The core interactive motif and its position are denoted. ( D ) The interaction of the indicated pairs of fused polypeptides (BD, binding domain; AD, activation domain of GAL4 transcription factor) was assayed as in C (GIP130, GPBP-interacting protein 130-kDa, residues 86–350). Blue color (+). ( E ) The indicated FLAG-tagged polypeptides were expressed, purified and analyzed by high-performance liquid chromatography (HPLC)-SEC. (A, E) Chromatograms are representative of at least three independent experiments.

    Journal: Oncotarget

    Article Title: Selective targeting of collagen IV in the cancer cell microenvironment reduces tumor burden

    doi: 10.18632/oncotarget.24280

    Figure Lengend Snippet: The druggable GPBP isoform is a multimer stabilized by self-interacting 260 SHCIE 264 motif ( A ) The indicated recombinant GPBP pools were analyzed by fast protein liquid chromatography (FPLC)-SEC. Calibrators, MW (kDa) and elution volumes (mL) were: thyroglobulin (669, 6.86), aldolase (158, 12.35) and serum human albumin (66, 13.89). In all chromatograms, the positions of the main GPBP oligomers are denoted. ( B ) Media (2.5 L) from the indicated cultures were affinity-purified using single-chain variable fragment (scFv)N26-column. Bound material was eluted in native conditions using N26-competing synthetic peptide (PS132) and analyzed as in A. Represented in AU are the FI of individual fractions in indirect ELISA analysis using anti-GPBP monoclonal antibodies (mAb). Shown is a representative assay of three. Image , mAb N27-developed WB of similarly purified (25 mL) GPBP eluted under denaturing conditions. Numbers and bars here and in following WB denote kDa and position of MW markers, respectively. ( C ) Structural features such as PH (empty box) and Start (scratched box) domains are indicated and represent GPBP and deletion mutants thereof. Indicated are spanning residues (numbers) and YTH interaction using colony-lift filter assays (+ or −). The core interactive motif and its position are denoted. ( D ) The interaction of the indicated pairs of fused polypeptides (BD, binding domain; AD, activation domain of GAL4 transcription factor) was assayed as in C (GIP130, GPBP-interacting protein 130-kDa, residues 86–350). Blue color (+). ( E ) The indicated FLAG-tagged polypeptides were expressed, purified and analyzed by high-performance liquid chromatography (HPLC)-SEC. (A, E) Chromatograms are representative of at least three independent experiments.

    Article Snippet: Fast protein liquid chromatography (FPLC)-SEC were performed using a Superdex 200 column (GE Healthcare) and high-performance liquid chromatography (HPLC)-SEC using a TSKgel® G4000SW column (Sigma-Aldrich).

    Techniques: Recombinant, Fast Protein Liquid Chromatography, Size-exclusion Chromatography, Affinity Purification, Indirect ELISA, Western Blot, Purification, Binding Assay, Activation Assay, High Performance Liquid Chromatography

    (A) Two-dimensional gel electropherogram of glutathione affinity chromatography fractions possessing GST activity. (B) Enlarged image of the boxed region showing grouping based on mass spectrometry fingerprints (refer to Table 1 ). IEF strip pI3-10NL was rehydrated in the protein precipitate from GST active fractions of the GSTrap column. This was focused for 48 kVh and then separated on a 10% polyacrylamide gel and stained with SYPRO Ruby.

    Journal: Journal of Experimental Botany

    Article Title: Purification, molecular cloning, and characterization of glutathione S-transferases (GSTs) from pigmented Vitis vinifera L. cell suspension cultures as putative anthocyanin transport proteins

    doi: 10.1093/jxb/ern217

    Figure Lengend Snippet: (A) Two-dimensional gel electropherogram of glutathione affinity chromatography fractions possessing GST activity. (B) Enlarged image of the boxed region showing grouping based on mass spectrometry fingerprints (refer to Table 1 ). IEF strip pI3-10NL was rehydrated in the protein precipitate from GST active fractions of the GSTrap column. This was focused for 48 kVh and then separated on a 10% polyacrylamide gel and stained with SYPRO Ruby.

    Article Snippet: Glutathione affinity chromatography Glutathione affinity chromatography was performed on the 60% ammonium sulphate precipitate of whole-cell protein extracted from day 5 cultures with GS-Trap columns (GE Healthcare) according to the manufacturer's instructions.

    Techniques: Two-Dimensional Gel Electrophoresis, Affinity Chromatography, Activity Assay, Mass Spectrometry, Electrofocusing, Stripping Membranes, Staining

    Purification of glutathione-binding proteins from pigmented V. vinifera cell suspension cultures. (A) Vitis vinifera FU-01 cells were cultured in GC-2 medium (filled circles) for 4 d, then elicited with 10 μM jasmonic acid, 20 g l −1 sucrose (or an equal volume of vehicle control), and constant white light irradiation (open circles, 96.8±2.2 μmol s −1 m −2 ). Cultures were incubated at 27±1 °C on a reciprocating shaker at 100 strokes min −1 , in 500 ml Erlenmeyer flasks containing 100 ml of B5 medium ( Gamborg et al. , 1968 ) supplemented with 30 g l −1 sucrose, 250 mg l −1 casein hydrolysate, 0.1 mg l −1 α-naphthaleneacetic acid, and 0.2 mg l −1 kinetin. GST activity, presented as the mean ±SD of three biological replicates performed in triplicate, was determined for the 60% ammonium sulphate precipitate ( n =9). (B) Sixty percent ammonium sulphate precipitate from day 5, non-elicited FU-01 line subjected to GST affinity chromatography. One-dimensional gel electropherogram of fractions (0.5 ml) from the GSTrap column. (C) Corresponding GST activity on the same fractions using CDNB as the model substrate.

    Journal: Journal of Experimental Botany

    Article Title: Purification, molecular cloning, and characterization of glutathione S-transferases (GSTs) from pigmented Vitis vinifera L. cell suspension cultures as putative anthocyanin transport proteins

    doi: 10.1093/jxb/ern217

    Figure Lengend Snippet: Purification of glutathione-binding proteins from pigmented V. vinifera cell suspension cultures. (A) Vitis vinifera FU-01 cells were cultured in GC-2 medium (filled circles) for 4 d, then elicited with 10 μM jasmonic acid, 20 g l −1 sucrose (or an equal volume of vehicle control), and constant white light irradiation (open circles, 96.8±2.2 μmol s −1 m −2 ). Cultures were incubated at 27±1 °C on a reciprocating shaker at 100 strokes min −1 , in 500 ml Erlenmeyer flasks containing 100 ml of B5 medium ( Gamborg et al. , 1968 ) supplemented with 30 g l −1 sucrose, 250 mg l −1 casein hydrolysate, 0.1 mg l −1 α-naphthaleneacetic acid, and 0.2 mg l −1 kinetin. GST activity, presented as the mean ±SD of three biological replicates performed in triplicate, was determined for the 60% ammonium sulphate precipitate ( n =9). (B) Sixty percent ammonium sulphate precipitate from day 5, non-elicited FU-01 line subjected to GST affinity chromatography. One-dimensional gel electropherogram of fractions (0.5 ml) from the GSTrap column. (C) Corresponding GST activity on the same fractions using CDNB as the model substrate.

    Article Snippet: Glutathione affinity chromatography Glutathione affinity chromatography was performed on the 60% ammonium sulphate precipitate of whole-cell protein extracted from day 5 cultures with GS-Trap columns (GE Healthcare) according to the manufacturer's instructions.

    Techniques: Purification, Binding Assay, Cell Culture, Irradiation, Incubation, Activity Assay, Affinity Chromatography

    Analytical heparin-Sepharose column elution profiles for thrombin, α 1 AT pitts , and their complex. A , elution profile of proteins and complexes, as indicated. It can be seen that α 1 AT pitts , native or cleaved ( peaks 1 and 4 ), does not bind

    Journal: The Journal of Biological Chemistry

    Article Title: Thrombin Inhibition by Serpins Disrupts Exosite II *

    doi: 10.1074/jbc.M110.144964

    Figure Lengend Snippet: Analytical heparin-Sepharose column elution profiles for thrombin, α 1 AT pitts , and their complex. A , elution profile of proteins and complexes, as indicated. It can be seen that α 1 AT pitts , native or cleaved ( peaks 1 and 4 ), does not bind

    Article Snippet: Heparin-Sepharose chromatography was conducted on a 1-ml HiTrap heparin-Sepharose column (GE Healthcare, Uppsala, Sweden).

    Techniques:

    Analytical Heparin-Sepharose Chromatography

    Journal: The Journal of Biological Chemistry

    Article Title: Thrombin Inhibition by Serpins Disrupts Exosite II *

    doi: 10.1074/jbc.M110.144964

    Figure Lengend Snippet: Analytical Heparin-Sepharose Chromatography

    Article Snippet: Heparin-Sepharose chromatography was conducted on a 1-ml HiTrap heparin-Sepharose column (GE Healthcare, Uppsala, Sweden).

    Techniques: Chromatography