Enzymatic Arginylation of @=Melanocyte-stimulating Hormone and of Angiotensin II*
نویسنده
چکیده
Porcine /3-melanocyte-stimulating hormone and angiotensin II were examixied as acceptors in the reaction catalyzed by arginyl-tRNA-protein transferase. Both inhibited enzymatic transfer of [l%]arginine from tRNA to bovine albumin. Inhibition was competitive with albumin and the Ki values were, respectively, 15 and 0.8 PM. The expected arginylated compounds were isolated and characterized. &Melanocyte-stimulating hormone and its arginylated product had identical activities in the frog epithelium bioassay. In contrast, the biological activity of angiotensin II was diminished by enzymatic arginylation. The pressor effect of the arginylated derivative on anesthetized rats and its activity on the isolated rat uterus were, respectively, approximately 60% and 20% of those found for the unmodified peptide.
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