The quantitative measurement of whey proteins using polyacrylamide-gel electrophoresis
- 1 February 1976
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 43 (2) , 259-265
- https://doi.org/10.1017/s0022029900015818
Abstract
Summary: A method is described for the quantitative estimation of a mixture of whey proteins by spectrophotometric scanning of the stained protein bands following polyacrylamide-gel electrophoresis. The incorporation of β-lactoglobulin A as an internal standard improves the accuracy of the technique. The method has been used to measure residual native whey proteins in milk after heating. Results are presented for whey protein denaturation in skim-milk after heat treatment at 130 and 140 °C for various periods of time.This publication has 12 references indexed in Scilit:
- Some quantitative aspects of the disc electrophoresis of ovalbumin using amido black 10B stainAnalytical Biochemistry, 1974
- Fluorometric scanning of fluorescamine-labeled proteins in polyacrylamide gelsAnalytical Biochemistry, 1974
- Quantitation of stained proteins in polyacrylamide gelsAnalytical Biochemistry, 1974
- An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie Brilliant BlueAnalytical Biochemistry, 1972
- Fluorescence monitoring of unstained protein bands in acrylamide gelAnalytical Biochemistry, 1971
- Scanning gel isoelectrofocusing of proteinsAnalytical Biochemistry, 1971
- The denaturation of α-lactalbumin and β-lactoglobulin in heated milkJournal of Dairy Research, 1970
- The electrophoresis of histones in polyacrylamide gel and their quantitative determinationBiochemical Journal, 1967
- A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresisAnalytical Biochemistry, 1967
- Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow's milkBiochemical Journal, 1957