Isolation of membrane-bound renal kallikrein and kininase

Author:

Ward P E1,Gedney C D2,Dowben R M3,Erdös E G4

Affiliation:

1. Departments of Pharmacology, University of Texas Health Science Center at Dallas, Tex. 75235, U.S.A

2. Departments of Internal Medicine, University of Texas Health Science Center at Dallas, Tex. 75235, U.S.A

3. Departments of Biophysics, University of Texas Health Science Center at Dallas, Tex. 75235, U.S.A

4. Departments of Physiology, University of Texas Health Science Center at Dallas, Tex. 75235, U.S.A

Abstract

Fractions highly enriched in plasma membrane, endoplasmic reticulum or brush border were prepared from homogenized rat kidney cortex. Kallikrein was concentrated in the plasma-membrane fraction, but not in the brush border of the proximal tubules. Kininase II or angiotensin I-converting enzyme was localized in the brush-border membrane. It is suggested that kallikrein in the urine may originate from the plasma membrane of the distal tubules and the conversion of angiotensin I and the inactivation of bradykinin may occur on the lumen membrane of the proximal tubular cells.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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