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 (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.
D001081:Apyrase / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D002846:Chromatography, Affinity; D007887:Fabaceae / Q000201:enzymology; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*; D010946:Plants, Medicinal; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D010744:Phosphoric Monoester Hydrolases; D001081:Apyrase