马肾激肽释放酶的纯化及其与马尿激肽释放酶的化学关系。

Purification of horse renal kallikrein and chemical relations with horse urinary kallikrein.

作者信息

Porcelli G, Marini-Bettolo G B, Croxatto H R, Di Jorio M

出版信息

Adv Exp Med Biol. 1979;120A:325-33. doi: 10.1007/978-1-4757-0926-1_31.

Abstract

Kallikrein was purified from horse kidney by several steps of chromatographic procedure and by affinity chromatography on Sepharose-Concanavaline. Horse urinary kallikrein was previously purified by DE-32 hydroxylapatite and by Sephadex G-100 gel filtration. On the purified final sample of renal and urinary kallikrein the aminoacid composition and the gel electrophoretic molecular weight were determined. The ratio in micronMoles between each aminoacid residue of both hydrolyzed renal and urinary kallikrein of horse is about 1,00 +/- 0,30. Except for Pro, 1/2 Cys and basic aminoacid residues a good proportion was obtained. It is confirmed that the different molecular weight, respectively 47,500 for renal kallikrein and 28,000 for the urinary enzyme is an artefact of the different procedures used for the purification of horse kallikrein.

摘要

通过几步色谱法以及在琼脂糖-伴刀豆球蛋白上进行亲和色谱，从马肾中纯化激肽释放酶。马尿激肽释放酶先前已通过DE-32羟基磷灰石和葡聚糖凝胶G-100凝胶过滤进行纯化。对纯化后的肾和尿激肽释放酶最终样品测定了氨基酸组成和凝胶电泳分子量。马肾和尿激肽释放酶水解后各氨基酸残基的微摩尔比约为1.00±0.30。除了脯氨酸、半胱氨酸和碱性氨基酸残基外，获得了良好的比例。证实了肾激肽释放酶分子量为47,500，尿激肽释放酶分子量为28,000，这种差异是用于纯化马激肽释放酶的不同方法造成的假象。