Abstract
The proteins soluble at low ionic strength of various muscles and of other tissues from five species of birds were examined by vertical starch-gel electrophoresis. The methods used were simple, and gave excellent and repeatable electrophoretic resolution of proteins. Most samples yielded 15–25 zones which stained nonspecifically for protein. Histochemical techniques revealed additional, enzyme, bands which were not coincident with the "major" protein zones. The results confirm and extend previous observations of the species specificity of the electrophoretic profiles of proteins from muscle extracts (myogen), and reveal considerable tissue and individual specificity of the enzymes and other proteins in extracts of avian tissues.
Publisher
Canadian Science Publishing
Cited by
6 articles.
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