Abstract
An aminopeptidase specific for N-terminal alanine was isolated from the rainbow trout (Oncorhynchus mykiss) maturing eggs using a simple procedure. The enzyme is composed of two identical units each of MW 16 000, separable by disulfide reduction. The enzyme has a high content of acid amino acids and its N-terminal sequence is the following 1EVNAVKCSMV10RDTLTTFNNK20KYQIN25. The sequence is identical with that of the rainbow trout vitellogenin precursor beginning with the amino acid in position 1 385. No peptidase activity has been so far observed in proteins derived from this precursor. The enzyme activity is partially blocked by Na4-EDTA but it is not inactivated by 4-(chloromercuri)benzoate, phenylmethanesulfonyl fluoride or pepstatin A.
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