1977
DOI: 10.1016/0003-2697(77)90197-x
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A new staining technique for proteins in polyacrylamide gels using Coomassie brilliant blue G250

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Cited by 827 publications
(339 citation statements)
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“…Urea gel electrophoresis was performed on the insoluble fractions of the control and the MF cheese samples stored in pH 4.6 buffer, after 1-, 15-, 30-, 45-, and 60-day aging time, using a Protean II vertical slab gel unit (Bio-Rad Laboratories Ltd.) and the stacking gel system described in the method of Blakesley and Boezi [3].…”
Section: Evaluation Of Proteolysismentioning
confidence: 99%
“…Urea gel electrophoresis was performed on the insoluble fractions of the control and the MF cheese samples stored in pH 4.6 buffer, after 1-, 15-, 30-, 45-, and 60-day aging time, using a Protean II vertical slab gel unit (Bio-Rad Laboratories Ltd.) and the stacking gel system described in the method of Blakesley and Boezi [3].…”
Section: Evaluation Of Proteolysismentioning
confidence: 99%
“…Proteins were dissociated by boiling in a solution containing 2.5 ~ (w/v) SDS, 10 ~ (v/v) glycerol, 5 ~ (v/v) 2-mercaptoethanol, and 0.002~o (w/v) bromophenol blue dye. Peptide bands were fixed and visualized by Coomassie Brilliant Blue G-250 staining (Blakesley & Boezi, 1977). Gels were destained in water, impregnated with Enhance, dried, and autoradiographed using Kodak X-Omat R (XR-5) X-ray film.…”
Section: Materials L-[3h]leucine L-mentioning
confidence: 99%
“…When fluorography was required, 10% polyacrylamide gel electrophoresis (PAGE) was performed in the same buffer, in which case proteins CMb and CMc are not well separated from each other. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) was carried out according to Laemmli (1970) and gels stained with Coomassie Brilliant Blue G-250 according to Blakesley and Boezi (1977). Fluorography was Incorporation in endosperm at 3 h: 230,000 total cpm mg" 1 ; 50,000 trichloroacetic acid (TCA) insoluble cpm mg" 1 .…”
Section: Electrophoresis and Fluorographymentioning
confidence: 99%