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一种用于分离人尿激肽释放酶的简单高产方法。

A simple high-yield procedure for isolation of human urinary kallikreins.

作者信息

Oza N B, Ryan J W

出版信息

Biochem J. 1978 Apr 1;171(1):285-8. doi: 10.1042/bj1710285.

Abstract

Two human urinary kallikreins (fractions A-1 and A-2) were purified to apparently homogeneous forms. The two kallikreins were separated by affinity chromatography using Trasylol (aprotinin) covalently bound to Sepharose. The kallikreins were eluted with a pH gradient (pH 9.5-3.0). Fraction A-1 was eluted between pH 6.2 and 4.2 and fraction A-2 was eluted between pH 4.2 and 3.1. Final purification was obtained by chromatography on Sephacryl SS-200. Antibodies prepared against fraction A-2 were also reactive with fraction A-1; thus it may be possible to measure both by radioimmunoassay using the same antibody preparation.

摘要

两种人尿激肽释放酶(A - 1和A - 2组分)被纯化至明显的均一形式。使用共价结合到琼脂糖上的抑肽酶通过亲和色谱法分离这两种激肽释放酶。激肽释放酶用pH梯度(pH 9.5 - 3.0)洗脱。A - 1组分在pH 6.2至4.2之间洗脱,A - 2组分在pH 4.2至3.1之间洗脱。通过在Sephacryl SS - 200上进行色谱法获得最终纯化。针对A - 2组分制备的抗体也与A - 1组分反应;因此,有可能使用相同的抗体制剂通过放射免疫测定法同时测量两者。

相似文献

3
Isolation and characterization of human urinary kallikrein.人尿激肽释放酶的分离与鉴定
Hoppe Seylers Z Physiol Chem. 1980 Jul;361(7):1003-16. doi: 10.1515/bchm2.1980.361.2.1003.

本文引用的文献

8
Synthesis of kallikreins by rat kidney slices.大鼠肾切片对激肽释放酶的合成
Br J Pharmacol. 1975 Feb;53(2):229-34. doi: 10.1111/j.1476-5381.1975.tb07353.x.
9

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