A calcium ion-dependent adenosine triphosphate pyrophosphohydrolase in plasma membrane from rat liver. Demonstration that the adenosine triphosphate analogues adenosine 5′-[βγ-imido]triphosphate and adenosine 5′-[βγ-methylene]-triphosphate are substrates for the enzyme
- 1 June 1978
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 171 (3), 817-820
- https://doi.org/10.1042/bj1710817
Abstract
An ATP pyrophosphohydrolase in a rat liver plasma-membrane subfraction was studied with respect to specific Ca2+ activation of the beta-phosphate bond hydrolysis. ATP and, in addition, adenosine 5′-[betagamma-imido]triphosphate and adenosine 5′-[betagamma-methlylene]triphosphate were substrates for Ca2+-stimulated enzymic hydrolysis of the beta-phosphate bond. A 15-fold activation was observed by raising the free Ca2+ concentration from 10(-7) to 10(-5) M. Mg2+ had little effect. Solubilization in 1% deoxycholate and partial purification on a sucrose density gradient resulted in a 5-fold increase in specific activity with unaltered Ca2+-stimulation pattern. The possible importance of the enzyme in Ca2+ transport is discussed.This publication has 11 references indexed in Scilit:
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