The hog intestinal mucosa acylase I: Subcellular localization, isolation, kinetic studies and biological function

摘要

The soluble acylase I (N_acylamino acid amidohydrolase, EC 3.5.1.14) from hog intestinal mucosa was 11 000-fold purified for the first time using a new four-step procedure involving an immunoaffinity chromatography. The resulting protein, which had an isoelectric point of 5.2 and a Mr of 90 000 was composed of two apparently identical N-acylated polypeptide chains. Its amino acid composition was comparable to that of hog kidney acylase I. The enzyme had a pH optimum at 8.0 and required Zn~2+ or CO~2+.