大鼠骨骼中紫色酸性磷酸酶的纯化与特性分析

Purification and characterization of purple acid phosphatase from rat bone.

作者信息

Kato T, Hara A, Nakayama T, Sawada H, Hamatake M, Matsumoto Y

出版信息

Comp Biochem Physiol B. 1986;83(4):813-7. doi: 10.1016/0305-0491(86)90152-5.

Abstract

An acid phosphatase, which was immunochemically identical to splenic purple acid phosphatase, was purified to homogeneity from rat bone. The enzyme was a two iron-containing monomeric glycoprotein with a mol. wt of 36,000. The enzyme hydrolyzed aryl phosphates, nucleoside di- and triphosphates, thiamine pyrophosphate, phosphoenolpyruvic acid and acidic phosphoproteins. The enzyme was inhibited by ammonium molybdate, NaF and CuSO4 but not by tartrate and SH-reagents.

摘要

一种酸性磷酸酶从大鼠骨骼中被纯化至同质，其免疫化学性质与脾脏紫色酸性磷酸酶相同。该酶是一种含两个铁原子的单体糖蛋白，分子量为36,000。该酶可水解芳基磷酸盐、核苷二磷酸和三磷酸、硫胺素焦磷酸、磷酸烯醇丙酮酸和酸性磷蛋白。该酶受到钼酸铵、氟化钠和硫酸铜的抑制，但不受酒石酸盐和巯基试剂的抑制。