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  • Title: Purification and properties of an aminopeptidase from the mid-gut gland of scallop (Patinopecten yessoensis).
    Author: Umetsu H, Arai M, Ota T, Kudo R, Sugiura H, Ishiyama H, Sasaki K.
    Journal: Comp Biochem Physiol B Biochem Mol Biol; 2003 Dec; 136(4):935-42. PubMed ID: 14662315.
    Abstract:
    An aminopeptidase was isolated from the mid-gut gland of Patinopecten yessoensis. The enzyme was purified from an acetone-dried preparation by extracting, ammonium sulfate precipitation, Hi-Load Q column chromatography, isoelectric focusing, and POROS HP2 and HQ column chromatography. The molecular weight of the enzyme was estimated to be 61 kDa by SDS-polyacrylamide gel electrophoresis and 59 kDa by gel permeation chromatography. The isoelectric point of the enzyme was 5.2 and the optimum pH was 7.0 toward leucine p-nitroanilide (Leu-pNA). The enzyme was inhibited by o-phenanthroline. The activity of the enzyme treated with o-phenanthroline was completely recovered by adding excess Zn(2+). Relative hydrolysis rates of amino acid-pNAs and amino acid-4-methylcoumaryl-7-amides (amino acid-MCAs) indicated that the enzyme preferred substrates having Ala or Met as an amino acid residue. The enzyme had a K(m) of 32.2 microM and k(cat) of 29.5 s(-1) with Ala-pNA and a K(m) of 11.1 microM and k(cat) of 9.49 s(-1) with Ala-MCA. The enzyme sequentially liberated amino acids from the amino-termini of Ala-Phe-Tyr-Glu.
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