Metalloenzyme inhibitor from kidney beans: partial purification and characterization

Metalloenzyme inhibitor from kidney beans: partial purification and characterization

Inhibitory activity directed against metalloenzymes has been highly purified from extracts of red kidney beans (Phaseolus vulgaris.) The inhibitor is a substance of small molecular weight and appears to be a chelator of Zn2+. One milligram of the preparation inhibited 23 milligrams carboxypeptidase...

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Veröffentlicht in:Plant physiology (Bethesda) 1979-03, Vol.63 (3), p.562-566
Hauptverfasser: Hojima, Y, Moriya, H, Moriwaki, C
Format: Artikel
Sprache:eng
Schlagworte:
Beans
Electrophoresis
Elution
Enzymes
Gels
Kidneys
Phosphatases
Plants
Precipitates
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creator Hojima, Y
Moriya, H
Moriwaki, C
description Inhibitory activity directed against metalloenzymes has been highly purified from extracts of red kidney beans (Phaseolus vulgaris.) The inhibitor is a substance of small molecular weight and appears to be a chelator of Zn2+. One milligram of the preparation inhibited 23 milligrams carboxypeptidase A. The inhibitor also strongly inhibited carboxypeptidase B and alkaline phosphatase and could activate phosphoglucomutase that had previously been inactivated with Zn2+. The isoelectric point of the inhibitor is 4.7. The inhibitor activity was abolished by preincubation with Zn2+,Ni2+, Co2+, or Cu2+. The mechanism of inhibition of carboxypeptidases and alkaline phosphatase by the bean inhibitor is apparently due to the complexing and complete removal of Zn2+ from the enzymes.
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source JSTOR Archive Collection A-Z Listing; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects Beans
Electrophoresis
Elution
Enzymes
Gels
Kidneys
Phosphatases
Plants
Precipitates
title Metalloenzyme inhibitor from kidney beans: partial purification and characterization
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