Jahreis G, Sorger H, Aurich H
Institut für Biochemie, Bereich Medizin, Martin-Luther-Universität Halle-Wittenberg.
Biomed Biochim Acta. 1989;48(9):617-24.
The alanine aminopeptidase of Acinetobacter calcoaceticus was found to be bound to the inner membranes only. The enzyme was solubilized by Triton X-100 and purified approximately 480-fold by gel filtration and affinity chromatography on alanine methyl ketone-AH-Sepharose 4B. The purified alanine aminopeptidase has a molecular mass of 212 kDa, estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme selectively catalyses the hydrolysis of N-terminal alanine residues of peptides. The enzyme is inhibited by p-hydroxy-mercuribenzoate, 1,10-phenanthroline, and puromycin, but was activated by CO2(+)-ions.
已发现醋酸钙不动杆菌的丙氨酸氨肽酶仅与内膜结合。该酶用 Triton X-100 增溶，并通过凝胶过滤和在丙氨酸甲基酮-AH-琼脂糖 4B 上的亲和层析纯化了约 480 倍。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计，纯化的丙氨酸氨肽酶的分子量为 212 kDa。该酶选择性地催化肽的 N 端丙氨酸残基的水解。该酶受到对羟基汞苯甲酸、1,10-菲咯啉和嘌呤霉素的抑制，但被 CO2(+)离子激活。
