Purification and Characterization of a Neutral Protease from Rat-Liver Cytosolic Fraction

Rat liver cytosol contains a neutral protease which degrades acetylated hemoglobin and some urea-denatured proteins maximally at pH 7.5. The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthr...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1987-11, Vol.102 (5), p.985-992
Main Authors: HIROI, Yuzo, NATORI, Yasuo
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cations, Divalent
Chromatography
Chromatography, Gel
Cytosol - enzymology
Edetic Acid - pharmacology
Endopeptidases - isolation & purification
Enzyme Activation - drug effects
Enzyme Reactivators
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Hydrolases
Liver - enzymology
livers
Male
Metals - pharmacology
Molecular Weight
Neprilysin
neutral proteinase
Phenanthrolines - pharmacology
Protease Inhibitors
proteinase
Rats
Rats, Inbred Strains
Substrate Specificity
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Summary:Rat liver cytosol contains a neutral protease which degrades acetylated hemoglobin and some urea-denatured proteins maximally at pH 7.5. The enzyme was purified to homogeneity by conventional chromatographic techniques. It appears to be a metalloprotease since it is inhibited by EDTA and o-phenanthroline, the metaldepleted enzyme can be reactivated by Co2+, Zn2+, Mn2+, or Mg2+, and it is not inhibited by reagents specific for carboxyl, seryl, or thiol proteases. The enzyme has an apparent molecular weight of 200,000 as determined on Sephacryl S-200 column chromatography, and electrophoresis in sodium dodecyl sulfate showed 3 protein bands corresponding to the molecular weights of 110,000, 74,000, and 40,000.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122175