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The primary structure of leucine amino peptidase ec from bovine eye lens

, : The primary structure of leucine amino peptidase ec from bovine eye lens. Journal of Biological Chemistry 257(12): 7077-7085

The amino acid sequence of bovine eye lens leucine aminopeptidase was determined. Cyanogen bromide fragments, the COOH-terminal hydroxylamine fragment and a large fragment obtained by digestion with Staphylococcus aureus protease were isolated from reduced and S-alkylated leucine aminopeptidase. The amino acid sequences of these fragments were determined by automated sequence analysis, by manual direct Edman degradation and by the dansyl-Edman technique. Overlapping peptides were obtained by tryptic digestion of the S-alkylated protein or the citraconylated S-alkylated protein. The polypeptide chain of leucine aminopeptidase comprises 478 residues, corresponding to a MW of 51,691. No significant sequence homology with any other published protein primary structure could be detected. This is the 1st report of a complete amino acid sequence of an enzyme belonging to the class of 2-metal peptidases.

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