bio rad model 620 video densitometer Search Results


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Bio-Rad densitometry
Figure 1. Chromatographic purification of E. coli oh8Gua endonuclease. After removal of nucleic acids with streptomycin, crude extract was separated by first phenyl HPLC (A), DEAE HPLC (B), gel filtration chromatography (C), second phenyl HPLC (D) and heparin affinity HPLC (E). For activity assay, 5 or 10 µl of each fraction was incubated with 5’ end-labeled substrate DNA containing oh8Gua. DNA nick at the site of oh8Gua was visualized with sequencing gel electrophoresis and autoradiography. For collection of active fractions, percentage of cleavage was determined by <t>densitometry.</t> Solid line, dashed line and dotted solid line indicate absorbance at 280 nm (protein profile; arbitrary unit except gel filtration chromatography), salt concentration and activity (% of nick), respectively.
Densitometry, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ceramic hydroxyapatite
Figure 1. Chromatographic purification of E. coli oh8Gua endonuclease. After removal of nucleic acids with streptomycin, crude extract was separated by first phenyl HPLC (A), DEAE HPLC (B), gel filtration chromatography (C), second phenyl HPLC (D) and heparin affinity HPLC (E). For activity assay, 5 or 10 µl of each fraction was incubated with 5’ end-labeled substrate DNA containing oh8Gua. DNA nick at the site of oh8Gua was visualized with sequencing gel electrophoresis and autoradiography. For collection of active fractions, percentage of cleavage was determined by <t>densitometry.</t> Solid line, dashed line and dotted solid line indicate absorbance at 280 nm (protein profile; arbitrary unit except gel filtration chromatography), salt concentration and activity (% of nick), respectively.
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Figure 1. Chromatographic purification of E. coli oh8Gua endonuclease. After removal of nucleic acids with streptomycin, crude extract was separated by first phenyl HPLC (A), DEAE HPLC (B), gel filtration chromatography (C), second phenyl HPLC (D) and heparin affinity HPLC (E). For activity assay, 5 or 10 µl of each fraction was incubated with 5’ end-labeled substrate DNA containing oh8Gua. DNA nick at the site of oh8Gua was visualized with sequencing gel electrophoresis and autoradiography. For collection of active fractions, percentage of cleavage was determined by <t>densitometry.</t> Solid line, dashed line and dotted solid line indicate absorbance at 280 nm (protein profile; arbitrary unit except gel filtration chromatography), salt concentration and activity (% of nick), respectively.
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Bio-Rad electrophoresis apparatus
(A) Two-dimensional gel <t>electrophoresis</t> of Leishmania membrane proteins (LAg). 51, 55 and 63 kDa spots were picked and subjected to tryptic digestion. (B) 63, 55 and 51 kDa proteins of LAg were electroeluted and subjected to SDS-PAGE. Corresponding lanes in part B was part of a single gel.
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Bio-Rad bio rad cfx manager 3 0 software
(A) Two-dimensional gel <t>electrophoresis</t> of Leishmania membrane proteins (LAg). 51, 55 and 63 kDa spots were picked and subjected to tryptic digestion. (B) 63, 55 and 51 kDa proteins of LAg were electroeluted and subjected to SDS-PAGE. Corresponding lanes in part B was part of a single gel.
Bio Rad Cfx Manager 3 0 Software, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad quantity one software
(A) Two-dimensional gel <t>electrophoresis</t> of Leishmania membrane proteins (LAg). 51, 55 and 63 kDa spots were picked and subjected to tryptic digestion. (B) 63, 55 and 51 kDa proteins of LAg were electroeluted and subjected to SDS-PAGE. Corresponding lanes in part B was part of a single gel.
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Bio-Rad optical system software
(A) Two-dimensional gel <t>electrophoresis</t> of Leishmania membrane proteins (LAg). 51, 55 and 63 kDa spots were picked and subjected to tryptic digestion. (B) 63, 55 and 51 kDa proteins of LAg were electroeluted and subjected to SDS-PAGE. Corresponding lanes in part B was part of a single gel.
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Image Search Results


Figure 1. Chromatographic purification of E. coli oh8Gua endonuclease. After removal of nucleic acids with streptomycin, crude extract was separated by first phenyl HPLC (A), DEAE HPLC (B), gel filtration chromatography (C), second phenyl HPLC (D) and heparin affinity HPLC (E). For activity assay, 5 or 10 µl of each fraction was incubated with 5’ end-labeled substrate DNA containing oh8Gua. DNA nick at the site of oh8Gua was visualized with sequencing gel electrophoresis and autoradiography. For collection of active fractions, percentage of cleavage was determined by densitometry. Solid line, dashed line and dotted solid line indicate absorbance at 280 nm (protein profile; arbitrary unit except gel filtration chromatography), salt concentration and activity (% of nick), respectively.

Journal: Experimental & molecular medicine

Article Title: Identification of Escherichia coli 8-oxoguanine endonuclease.

doi: 10.1038/emm.2000.26

Figure Lengend Snippet: Figure 1. Chromatographic purification of E. coli oh8Gua endonuclease. After removal of nucleic acids with streptomycin, crude extract was separated by first phenyl HPLC (A), DEAE HPLC (B), gel filtration chromatography (C), second phenyl HPLC (D) and heparin affinity HPLC (E). For activity assay, 5 or 10 µl of each fraction was incubated with 5’ end-labeled substrate DNA containing oh8Gua. DNA nick at the site of oh8Gua was visualized with sequencing gel electrophoresis and autoradiography. For collection of active fractions, percentage of cleavage was determined by densitometry. Solid line, dashed line and dotted solid line indicate absorbance at 280 nm (protein profile; arbitrary unit except gel filtration chromatography), salt concentration and activity (% of nick), respectively.

Article Snippet: To determine the collection of active fractions, % of DNA breakage was estimated by densitometry (Model 620, BioRad, USA).

Techniques: Purification, Filtration, Chromatography, Activity Assay, Incubation, Labeling, Sequencing, Nucleic Acid Electrophoresis, Autoradiography, Concentration Assay

(A) Two-dimensional gel electrophoresis of Leishmania membrane proteins (LAg). 51, 55 and 63 kDa spots were picked and subjected to tryptic digestion. (B) 63, 55 and 51 kDa proteins of LAg were electroeluted and subjected to SDS-PAGE. Corresponding lanes in part B was part of a single gel.

Journal: Scientific Reports

Article Title: Immunoproteomic Identification and Characterization of Leishmania Membrane Proteins as Non-Invasive Diagnostic Candidates for Clinical Visceral Leishmaniasis

doi: 10.1038/s41598-018-30546-y

Figure Lengend Snippet: (A) Two-dimensional gel electrophoresis of Leishmania membrane proteins (LAg). 51, 55 and 63 kDa spots were picked and subjected to tryptic digestion. (B) 63, 55 and 51 kDa proteins of LAg were electroeluted and subjected to SDS-PAGE. Corresponding lanes in part B was part of a single gel.

Article Snippet: Excised protein bands were eluted using electrophoresis apparatus (BioRad, Model-422) under running buffer (1% SDS, 0.192 M glycine and 0.025 M Tris) for 4 h at 10 mA.

Techniques: Two-Dimensional Gel Electrophoresis, Electrophoresis, Membrane, SDS Page