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通过高分辨率离子交换色谱法纯化胃蛋白酶原A同工酶。翻译后修饰的证据。

Purification of the pepsinogen A isozymogens by means of high resolution ion-exchange chromatography. Evidence for post-translational modifications.

作者信息

Défize J, Pals G, Pronk J C, Frants R R, Rimmelzwaan G, Westerveld B D, Eriksson A W

出版信息

Scand J Clin Lab Invest. 1985 Nov;45(7):649-55. doi: 10.3109/00365518509155273.

Abstract

Total human pepsinogen (PG) was isolated from gastric fundic mucosa and PGA (formerly called PGI) from urine, using standard ion-exchange and gel filtration techniques. Gastric PGA was separated from PGC (formerly called PGII) either by immunoaffinity or high resolution ion-exchange chromatography (fast protein liquid chromatography, Pharmacia, Uppsala, Sweden). The individual PGA isozymogens 2, 3, 4 and 5 could be isolated to homogeneity with the aid of the same ion-exchanger. Evidence was obtained for the existence of secondary modifications of the PGA fractions 3, 4 and 5, electrophoretically overlapping the primary (genetic) isozymogens.

摘要

采用标准离子交换和凝胶过滤技术,从胃底黏膜中分离出总人胃蛋白酶原(PG),从尿液中分离出胃蛋白酶原A(以前称为PGI)。胃蛋白酶原A通过免疫亲和或高分辨率离子交换色谱法(快速蛋白质液相色谱法,瑞典乌普萨拉法玛西亚公司)与胃蛋白酶原C(以前称为PGII)分离。借助相同的离子交换剂,可将各个胃蛋白酶原A同工酶2、3、4和5分离至均一状态。有证据表明,胃蛋白酶原A组分3、4和5存在二级修饰,在电泳上与主要(遗传)同工酶重叠。

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