The primary structure of leucine aminopeptidase from bovine eye lens.
The amino acid sequence of bovine eye lens leucine aminopeptidase has been 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 molecular weight of 51,691. No significant sequence homology with any other published protein primary structure could be detected. This is the first report of a complete amino acid sequence of an enzyme belonging to the class of two metal peptidases.
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases; D002417:Cattle; D003488:Cyanogen Bromide; D007908:Lens, Crystalline / Q000201:enzymology*; D007931:Leucyl Aminopeptidase; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D010446:Peptide Fragments; D002268:Carboxypeptidases; D007931:Leucyl Aminopeptidase; D014357:Trypsin; D003488:Cyanogen Bromide