Abstract
As a first step in our study of structure-function relationships among primate and non-primate growth hormones, human growth hormone (hGH) was subjected to the limited digestive activity of human plasmin. The lyophilized whole digest, containing less than 2% of unchanged hormone, had an average of 2.3 new amino-terminal groups per mole. The digest had the same potency as the native hormone (a) in causing weight gain in hypophysectomized rats; (b) in stimulating somatomedin production in hypophysectomized rats; (c) in stimulating upake of [3H]leucine into isolated diaphragm of hypophysectomized rats; (d) in accelerating transport of [14C]α-aminoisobutyric acid into isolated diaphragm of hypophysectomized rats; (e) in stimulating uptake of [3-0-methyl-14C]glucose by isolated adipose tissue of hypophysectomized rats; (f) in accelerating conversion of [14C]glucose to 14CO2 by isolated epididymal adipose tissue of hypophysectomized rats. The digest also caused glucosuria in partially pancreatectomized rats treated with dexamethasone.
Authors
John B. Mills, Charles R. Reagan, Daniel Rudman, Jack L. Kostyo, P. Zachariah, Alfred E. Wilhelmi
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