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The primary structure of leucine amino peptidase ec 3.4.11.1 from bovine eye lens


Journal of Biological Chemistry 257(12): 7077-7085
The primary structure of leucine amino peptidase ec 3.4.11.1 from bovine eye lens
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.


Accession: 006740933



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