Related Experiment Video
Updated: May 27, 2026

Exploring the Longissimus Muscle: Unraveling its Correlation with Meat Quality in Bos indicus and Crossbred Bulls
Published on: July 12, 2024
Quantification of beef myofibrillar proteins by SDS-PAGE
E Claeys1, L Uytterhaegen, B Buts
1Department of Animal Production, Gent University, Proefhoevestraat, 10, 9090 Melle, Belgium.
Abstract:
A semi-quantitative determination of beef myofibrillar proteins using sodium, dodecyl sulphate polyacrylamide gel electrophoresis is described. Bovine serum albumin was used as internal standard. Results indicate a linear relationship between densitometric readings after staining with Coomassie brilliant blue R(250) and protein content. Recoveries of four pure proteins, loaded within a range of 0·5-4 μg, were between 92 and 110%. Heating of beef myofibrillar protein samples during dissolution is shown to be unnecessary. The method allows the quantitative study of myofibrillar degradation during beef aging, without overlapping of troponin-T with tropomyosin bands.
Related Concept Videos
SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Two-dimensional Gel Electrophoresis
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...
Western Blotting
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.

