Abstract
Heterogeneity of bovine sarcoplasmic protein fractions obtained by DEAE-cellulose ion exchange chromatography was investigated by vertical polyacrylamide gel electrophoresis. Results of these electrophoretic analyses indicated that the five major chromatographic fractions were quite heterogeneous. Fraction areas I and III, which appeared as single chromatographic peaks, showed five and six distinct bands, respectively, when subjected to gel electrophoresis. The other chromatographic groups, fraction areas II, IV and V, were separated into five, eight and three electrophoretically different bands, respectively. Some possible reasons for the apparent chromatographic heterogeneity are discussed.
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Schedule a callMore From: Canadian Institute of Food Technology Journal/Journal de l'Institut canadien de technologie alimentaire
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