Conversion between renin and high-molecular-weight renin in the dog
- 15 December 1978
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 176 (3) , 977-981
- https://doi.org/10.1042/bj1760977
Abstract
Two forms of renin, one of mol.wt. 43,000 and the other 60,000, were found in the dog kidney. Conversion between the two forms of renin was reversible at neutral pH. Though the molecular weight of renin in kidney-cortex homogenate was 43,000, it was completely converted into high-molecular-weight renin in the presence of substances that react with thiol groups. On the contrary, stored renin in the granules was the form of normal size (mol. wt. 43,000) regardless of the absence or presence of such substances. The present experiments indicated that renin is stored in the granules as the form of normal size and might be converted into high-molecular-weight renin when it is released from the granules and attached to some substance in the soluble fraction of renal-cortical tissue.This publication has 12 references indexed in Scilit:
- Activation of Human Inactive (“Pro-”) Renin by Cathepsin D and Pepsin*Journal of Clinical Endocrinology & Metabolism, 1978
- Native form of renin in the kidney.Journal of Biological Chemistry, 1977
- Biochemical Properties of Big Renin Extracted from Human PlasmaJournal of Clinical Endocrinology & Metabolism, 1975
- Occurrence of Big Renin in Human Plasma, Amniotic Fluid and Kidney ExtractsJournal of Clinical Endocrinology & Metabolism, 1975
- A renin inhibitor from rabbit kidney: conversion of a large inactive renin to a smaller active enzyme.Circulation Research, 1975
- A Protein-Bound Form of Porcine Renal ReninCirculation Research, 1974
- Isolation of renin granules from the dog kidney cortex.Journal of Applied Physiology, 1972
- A RELEASE OF RENIN FROM DOG KIDNEY CORTEX SLICESThe Japanese Journal of Pharmacology, 1970
- Application of a Radioimmunoassay for Angiotensin I to the Physiologic Measurements of Plasma Renin Activity in Normal Human Subjects1Journal of Clinical Endocrinology & Metabolism, 1969
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951