Enzymic Inactivation of Oxytocin.

Abstract
By chromatography on DEAE-cellulose, retroplacental serum is shown to contain at least 2 enzymes having cystine aminopeptidase properties. The main component has the ability to hydrolyze at least the first 3 N-terminally situated peptide bonds of oxytocin, as evidenced by the amino acid composition, Edman degradation and thin-layer chromatography of the cleavage products. By chromatography on Sephadex G-200, oxytocinase is eluted between the "7 S-" and "11 S-components".
Keywords

This publication has 0 references indexed in Scilit: