CHARACTERISTICS OF DISCONTINUOUS STARCH GEL ELECTROPHORESIS APPLIED TO MYOGEN FROM CHICKEN BREAST MUSCLE

Abstract

The essential characteristics of discontinuous starch gel electrophoresis, introduced by Poulik (1), were studied by varying the compositions of gel and bridge buffers, by conductivity measurements within the gel during electrophoresis, and by examination of electropherograms of chicken breast myogen, a protein mixture prone to influence by the buffer medium. The obligatory ingredients of discontinuous buffer systems were Tris cation in the gel medium, and borate anion in the bridge solution. The cation of the bridge solution was immaterial, and any anion other than borate was adequate in the gel. A flux of borate, migrating through the gel across a matrix of Tris adsorbed to starch, profoundly reduced conductivity and displaced protein-ion complexes from the support phase in an electrochromatographic manner. Some new discontinuous systems are introduced, but despite the striking patterns obtained these conditions are not necessarily the most informative for starch gel electrophoresis of cationic proteins, including major components of myogen.