二氧化碳嗜纤维菌属细菌的酸性和碱性磷酸酶。II. 从赭色二氧化碳嗜纤维菌中分离、纯化及鉴定这些酶

Acid and alkaline phosphatases of Capnocytophaga species. II. Isolation, purification, and characterization of the enzymes from Capnocytophaga ochracea.

作者信息

Poirier T P, Holt S C

出版信息

Can J Microbiol. 1983 Oct;29(10):1361-8. doi: 10.1139/m83-211.

Abstract

Capnocytophaga ochracea acid (AcP; EC 3.1.3.2) and alkaline (AlP; EC 3.1.3.1) phosphatase was isolated by Ribi cell disruption and purified by sodium dodecyl sulphate - polyacrylamide gel electrophoresis (SDS-PAGE.) Both phosphatases eluted from Sephadex G-150 consistent with molecular weights (migration) of 140 000 and 110 000. SDS-PAGE demonstrated a 72 000 and 55 000 subunit molecular migration for AcP and AlP, respectively. The kinetics of activity of purified AcP and AlP on p-nitrophenol phosphate and phosphoseryl residues of the phosphoproteins are presented.

摘要

通过里比细胞破碎法分离出了黄褐二氧化碳嗜纤维菌酸性磷酸酶（AcP；EC 3.1.3.2）和碱性磷酸酶（AlP；EC 3.1.3.1），并通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）进行纯化。两种磷酸酶从葡聚糖凝胶G-150上洗脱下来，其分子量（迁移率）分别为140000和110000。SDS-PAGE显示，AcP和AlP的亚基分子量迁移率分别为72000和55000。文中给出了纯化后的AcP和AlP对磷酸对硝基苯酚和磷蛋白的磷酰丝氨酸残基的活性动力学。