Activation of Kidney Prorenin by Kidney Cathepsin B Isozymes1
- 1 January 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 91 (1) , 419-422
- https://doi.org/10.1093/oxfordjournals.jbchem.a133705
Abstract
Kidney prorenin was converted to a form of active renin by kidney cathepsin B isozymes. The three isozymes showed similar catalytic behavior for prorenin. The optimal pH for the activation was in the range of 4.0–5.0 and the reaction was completely inhibited by leupeptin. The molecular weight and the isoelectric point of the activated prorenin were 40,000 and pH 4.9. As a minor product, an activated prorenin having an isoelectric point of 5.2 was also produced.This publication has 8 references indexed in Scilit:
- Purification and Characterization of Porcine Kidney Cathepsin B1The Journal of Biochemistry, 1981
- Totally inactive renin zymogen and different forms of active renin in hog brain tissues.Journal of Biological Chemistry, 1981
- INTERMEDIATE MOLECULAR WEIGHT RENIN AND RENIN-BINDING PROTEIN(S) IN THE HOG KIDNEY Biomedical Research, 1980
- RENIN PRECURSOR IN HOG KIDNEY. OCCURRENCE AND PARTIAL CHARACTERIZATION Biomedical Research, 1980
- Isolation of completely inactive plasma prorenin and its activation by kallikreinsBiochimica et Biophysica Acta (BBA) - Enzymology, 1979
- Partial purification and chromatographic properties of inactive renin from human amniotic fluidBiochemical Pharmacology, 1979
- Calcium-dependent Golgi-vesicle fusion and cathepsin B in the conversion of proalbumin into albumin in rat liverBiochemical Journal, 1978
- Pure Renin. Isolation from hog kidney and characterization.Journal of Biological Chemistry, 1977