Collect. Czech. Chem. Commun.
2000, 65, 1198-1204
https://doi.org/10.1135/cccc20001198
Purification and Characterisation of a Vitellogenin Derived Aminopeptidase from Rainbow Trout Eggs
Jakub Kronovetra,b,*, Jana Barthováb, Tomislav Bartha and Helena Ryšlaváb
a Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic
b Department of Biochemistry, Faculty of Science, Charles University, 128 40 Prague 2, Czech Republic
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.
Keywords: Enzymes; Aminopeptidases; Fish eggs; 4-Nitroanilides; Rainbow trout; Vitellogenin.
References: 34 live references.
