Purification and characterization of a membrane-bound ATP diphosphohydrolase from Cicer arietinum (chick-pea)roots

Microsomal membranes from Cicer arietinum (chick-pea) roots contained an ATP phosphohydrolase activity that could be solubilized by high-ionic-strength media. The enzyme has been purified to homogeneity by affinity and ion-exchange chromatography. It has the properties of an ATP diphosphohydrolase (...

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Published inBiochemical journal Vol. 197; no. 3; pp. 637 - 643
Main Authors Vara, F, Serrano, R
Format Journal Article
LanguageEnglish
Published England 01.09.1981
Subjects
apyrase
Apyrase - isolation & purification
Apyrase - metabolism
Cell Membrane - enzymology
Chromatography, Affinity
Cicer arietinum
Fabaceae - enzymology
Kinetics
microsomes
Phosphoric Monoester Hydrolases - metabolism
Plants - enzymology
Plants, Medicinal
purification
Subcellular Fractions - enzymology
Substrate Specificity
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Summary:Microsomal membranes from Cicer arietinum (chick-pea) roots contained an ATP phosphohydrolase activity that could be solubilized by high-ionic-strength media. The enzyme has been purified to homogeneity by affinity and ion-exchange chromatography. It has the properties of an ATP diphosphohydrolase (apyrase, EC 3.6.1.5) that hydrolyses different nucleoside di- and tri-phosphates but has no activity towards monophosphoric esters and pyrophosphate. No stimulation by K+ could be demonstrated for either the membrane-bound or the purified enzyme, and therefore it would seem not to be related to the K+ -dependent ATPase postulated to mediate K+ transport in plants.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj1970637