Abstract
Proteinase activities of eggs and cells of the cumulus oophorous of the golden hamster were investigated with highly sensitive fluorogenic amide substrates. Eggs contain a neutral endopeptidase which hydrolyzed Suc-Ala-Ala-Phe-7-amino-4-methylcoumarin amide between the Ala and the Phe residues. Endopeptidase action on this substrate resulted in the accumulation of Phe-7-amino-4-methylcoumarin amide which was monitored by tlc identification. Hamster eggs also contained aminopeptidase and elastase-like activities but no detectable trypsin-like activity. Aminopeptidase, endopeptidase, trypsin-like, and elastase-like activities were detected in cumulus cells.
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