Heterogeneity of Porcine Somatotropin

Abstract
A chromatographic method is pressented by which highly purified porcine somatotropin can be separated preparatively into 5-subfractions. The rechromatograhped subfractions show comparable biological activities and molecular sizes, but they differ characteristically in the polyacrylamide gel electrophoresis and in the isoelectric focusing. Relatively small differences were found in the amino acid composition of these fractions. The question is discussed whether the term multiple forms or isohormones of porcine somatotropin is suitable for the growth promoting fractions.

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