青蛙肝脏中的低分子量酸性磷酸酶：具有不同生物活性糖型的同源酸性磷酸酶III和IV的分离

The lower molecular weight acid phosphatase from the frog liver: isolation of homogeneous AcPase III and IV representing glycoforms with different bioactivity.

Jańska H, Kubicz A, Szalewicz A

Institute of Biochemistry, University of Wrocław, Poland.

Comp Biochem Physiol B. 1989;92(2):341-6. doi: 10.1016/0305-0491(89)90288-5.

Abstract

AcPase III and AcPase IV, the major enzyme forms of the LMW AcPase of the frog (Rana esculenta) liver were resolved and purified to homogeneity. 2. AcPase III and IV showed a single protein band on SDS-PAGE corresponding to a mol. wt (Mr) of about 35,000. The Mr of the native enzyme forms were 33,200 (gel electrophoresis) and 38,200 +/- 5000 (gel filtration). This indicates that they are monomeric proteins sharing the same protein molecule. 3. AcPase III and IV differ essentially in thermostability and the activating effect of ConA binding. 4. AcPase III and IV are considerably activated with DTT but they differed markedly by the extent of this activation and the accompanying changes of their pH-activity curves. 5. It is suggested that the frog liver LMW AcPase represents a set of glycoforms whose different bioactivity is determined by the redox states of their essential cysteine residues.

摘要

蛙（食用蛙）肝脏低分子量酸性磷酸酶的主要酶形式酸性磷酸酶III和酸性磷酸酶IV被分离并纯化至同质。2. 酸性磷酸酶III和IV在SDS-PAGE上显示出一条单一蛋白带，对应分子量（Mr）约为35,000。天然酶形式的Mr为33,200（凝胶电泳）和38,200±5000（凝胶过滤）。这表明它们是共享相同蛋白质分子的单体蛋白。3. 酸性磷酸酶III和IV在热稳定性和伴刀豆球蛋白A结合的激活作用方面存在本质差异。4. 酸性磷酸酶III和IV被二硫苏糖醇显著激活，但它们在这种激活程度以及伴随的pH-活性曲线变化方面存在明显差异。5. 有人提出，蛙肝脏低分子量酸性磷酸酶代表一组糖型，其不同的生物活性由其必需半胱氨酸残基的氧化还原状态决定。