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脑苷脂硫酸酯酶激活剂。从人肝脏中纯化并鉴定为一种蛋白质。

The activator of cerebroside sulphatase. Purification from human liver and identification as a protein.

作者信息

Fischer G, Jatzkewitz H

出版信息

Hoppe Seylers Z Physiol Chem. 1975 May;356(5):605-13. doi: 10.1515/bchm2.1975.356.1.605.

Abstract
  1. A heat-stable activator of human sulphatase A (cerebroside sulphatase) was purified from human liver. It is required for the enzymatic degradation of cerebroside sulphates (sulphatides) in buffers (ionic strength greater than or equal 0.2) with osmolarity in the physiological range. 2) The purification steps involve extraction, acetone precipitation, heat treatment, isoelectric focusing and gel filtration. 3) Based on the definition of a specific activator unit, the purification of the final preparation was approximately 2000-fold over the acetone precipitation and several thousand-fold in the overall procedure. 4) The purified activator migrated as a single protein band when subjected to gel electrophoresis. Its effect was abolished after treatement with pronase E. The apparent molecular weight as determined by gel filtration was 21 500 +/- 1500; the isoelectric point was 4.3. 5) The activating effect of this protein factor and of taurodeoxycholate on cerebroside sulphatase activity was compared on a weight and molar basis.
摘要
  1. 从人肝脏中纯化出一种人硫酸酯酶A(脑苷脂硫酸酯酶)的热稳定激活剂。在渗透压处于生理范围的缓冲液(离子强度大于或等于0.2)中,脑苷脂硫酸盐(硫脂)的酶促降解需要该激活剂。2) 纯化步骤包括提取、丙酮沉淀、热处理、等电聚焦和凝胶过滤。3) 根据特定激活剂单位的定义,最终制剂的纯化程度相对于丙酮沉淀约为2000倍,在整个过程中为数千倍。4) 纯化后的激活剂在进行凝胶电泳时迁移为单一蛋白条带。用链霉蛋白酶E处理后其作用消失。通过凝胶过滤测定的表观分子量为21500±1500;等电点为4.3。5) 在重量和摩尔基础上比较了该蛋白质因子和牛磺去氧胆酸盐对脑苷脂硫酸酯酶活性的激活作用。

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