ENZYMATIC MODIFICATION OF BOVINE GROWTH HORMONE BY PROTEOLYTIC STREPTOMYCETE CELL EXTRACTS
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ABSTRACT Bovine growth hormone was subjected to enzymatic hydrolysis by several crude proteolytically active streptomycete cell extracts. These digestion mixtures were fractionated on Sephadex gel columns. With each enzyme substantial amounts of hormonal aggregational products were formed during enzymatic hydrolysis with an apparent molecular weight exceeding the one for the native hormone. Fractions obtained retained various degrees of somatotrophic, lipolytic, and immunologic activities. In the course of these investigations it became apparent that the prepared bovine growth hormone fragments had a high inorganic ion binding capacity, in particular for Na+, Mg++, and SiO3−−.