Abstract
The enzymatic cleavage of synthetic oxytocin and 8-lysine vasopressin by sera of women in advanced pregnancy was investigated by using paper chromatography. Following incubation of either hormone with pregnancy serum and subsequent oxidation, two molecular fractions were formed, of which one could be identified as L-cysteic acid. By contrast, oxidation of the intact cyclopeptide hormones did not lead to liberation of free L-cysteic acid. It was concluded that oxytocin and 8-lysine vasopressin were cleaved by an identical mechanism involving splitting of the peptide bond joining the tyrosine residue (position 2) to the amino-terminal half-cystine residue (position 1). Pregnancy serum "oxytocinase" and "vasopressinase" thus appeared to be one and the same enzyme.

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