Summary: The supernatant extracts from disrupted had only low hydrolytic activity towards diglycine, divaline and prolylglycine, but latent peptidases were activated by Co or Mn. The cations K, Mg, Zn, Fe, Ni, Cu Ca and Cd caused no increase in peptidase activity while Cd, Zn and Cu antagonized the effects of Co and Mn. Measurements of optimum cation concentration, of pH optimum and of effects of various buffers led to the conclusion that the main peptidase activity towards these three peptides, and towards a broad spectrum of other dipeptides, resided in a single Co activated enzyme. The activity of this peptidase was enhanced by phosphate and inhibited by veronal. Similar measurements with Mn suggested the presence of several enzymes with lower activities and narrower substrate specificity than the Co activated peptidase. Procedures were devised for the assay, under optimum conditions, of the main peptidase activities of a crude extract.


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