| Literature DB >> 2466651 |
Abstract
The proteins of cheese are rapidly solubilised by heating to 95 degrees C in buffered 2% sodium dodecyl sulfate, 5% 2-mercaptoethanol. Electrophoretic analysis of the solubilised proteins by either one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis or high resolution two-dimensional electrophoresis yields reproducible patterns characteristic of an individual cheese and its extent of ripening. The patterns reveal (i) the residual amounts of milk casein and whey proteins, and (ii) the appearance of casein degradation products, including pink-violet components as detected by Coomassie Blue staining.Entities:
Mesh:
Substances:
Year: 1988 PMID: 2466651 DOI: 10.1002/elps.1150090308
Source DB: PubMed Journal: Electrophoresis ISSN: 0173-0835 Impact factor: 3.535