Modification of lysine 69 reactivity in bovine growth hormone by carbamylation of its N-terminal group.

Abstract

Bovine growth hormone was carbamylated under conditions that assure full reaction of the N-terminal residue. Approximately 28% of lysine 179 and 7% of lysine 143 were also carbamylated. The modified hormone retained an important growth promoting activity and was as effective as the native hormone in competition assays in vivo for the receptors in rat liver. However, a change in its conformation must occur since lysine 69, which is resistant to trinitrophenylation in the native hormone, reacted easily and under mild conditions, in the carbamylated protein, The growth promoting activity and binding properties of the carbamylated and trinitrophenylated hormone were practically nil.