ANGIOTENSINASE-A (AMINOPEPTIDASE-A) - PROPERTIES OF CHROMATOGRAPHICALLY PURIFIED ISOFORMS FROM HUMAN KIDNEY

被引：12

作者：

HERZIG, CM ^{[1
]}

SCHOEPPE, W ^{[1
]}

SCHERBERICH, JE ^{[1
]}

机构：

[1] UNIV FRANKFURT,CTR INTERNAL MED,DEPT NEPHROL,THEODOR STERN KAI 7,W-6000 FRANKFURT 1,GERMANY

来源：

JOURNAL OF CHROMATOGRAPHY | 1992年 / 625卷 / 01期

关键词：

D O I：

10.1016/0021-9673(92)87223-U

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Angiotensin-II-cleaving angiotensinase A (aminopeptidase A, E.C. 3.4.11.7, ATA) plays an important role in glomerular haemodynamics, the pathophysiology of essential arterial hypertension and the induction of vascular disorders. In order to study biochemical and immunological properties of ATA, two isoforms (I and II) of the glycoprotein were isolated for the first time from human kidney cortex. Kidney cortex homogenate, digested with bromelain, was fractionated by ammonium sulphate precipitation and subsequent hydrophobic interaction chromatography, using a fast protein liquid chromatographic (FPLC) system. By anion-exchange FPLC (Mono Q column), the isoforms of ATA were eluted in two distinct peaks and were further purified by size-exclusion FPLC and preparative polyacrylamide gel electrophoresis. Biochemical, immunological and immunohistological characterization disclosed differences in the intrarenal localization, glycosylation, Michaelis constant and apparent molecular mass (native and sodium dodecyl sulphate gel electrophoresis) but similar properties in the double-immunodiffusion technique. Polyclonal rabbit antibodies, raised against ATA isoforms I and II, precipitated an analogous antigen in urine from patients with renal tubular damage.

引用

页码：73 / 82

页数：10