Differentiation of Semen from Bos Bubalus and Bos Taurus Indicus by Starch Gel Electrophoresis

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Abstract
Considerable differences in the electrophoretic pattern of the seminal plasma proteins of bovine and buffalo were observed using paper strip and starch gel electrophoresis. Better resolution of the protein components was observed in the case of bovine semen using paper strip electrophoresis whereas buffalo semen gave poorer resolution. Starch gel electrophoresis of bovine seminal plasma protein at alkaline pH revealed the presence of two distinct cathodic components in addition to four anodic components, whereas in buffalo semen, cathodic components were absent and anodic components, showed slower mobility. At acidic pH, bovine semen exhibited the presence of nine protein components (4 major) whereas six components were present in buffalo semen. Two of the faster moving components in the seminal plasma of bovine were absent in the buffalo seminal plasma. Gel filtration indicated considerable differences in the minor components of bovine and buffalo seminal plasma proteins. No variation in the electrophoretic resolution pattern was noticed within the bovine and buffalo populations. Compositional differences in the protein components of bovine and buffalo seminal plasma in relation to their characterization have been discussed. Copyright © 1971. American Society of Animal Science. Copyright 1971 by American Society of Animal Science.

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