M. W. Montgomery

Separation of Bovine Sarcoplasmic Proteins by Vertical Gel Electrophoresis

Abstract Vertical electrophoresis utilizing polyacrylamide gels varying in concentrations from 5 to 20% was employed to separate bovine sarcoplasmic proteins by both continuous and discontinuous techniques. Results of a series of electrophoretic runs indicated that a gel concentration of 10% was optimum for separating these proteins. In terms of resolution, reproducibility and sharpness of boundaries of the separated protein bands, the discontinuous technique was found to be superior to the continuous procedure. Electrophoresis of the sarcoplasmic extracts by the discontinuous technique resulted in the separation of 18 electrophoretically different sarcoplasmic proteins.

Electrophoretic Separation of Bovine Sarcoplasmic Proteins Fractionated by DEAE-Cellulose Chromatography

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.