Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase
- 1 January 1979
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 98 (1) , 41-47
- https://doi.org/10.1002/jcp.1040980106
Abstract
Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10−4, the Vmax = 1.2 × 10−9 and the Keq = 3.8 × 104. Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by phydroxymercuribenzoate.This publication has 12 references indexed in Scilit:
- THE COLORIMETRIC DETERMINATION OF PHOSPHORUSPublished by Elsevier ,2021
- ITP pyrophosphohydrolase and idp phosphohydrolase in rat tissueJournal of Cellular Physiology, 1975
- The distribution of nucleoside triphosphate pyrophosphohydrolase in the tissues of the rabbitArchives of Biochemistry and Biophysics, 1974
- Micro assay of ITP pyrophosphohydrolase by liquid scintillationAnalytical Biochemistry, 1972
- Human erythrocyte “ITPase”: An ITP pyrophosphohydrolaseBiochimica et Biophysica Acta (BBA) - General Subjects, 1970
- Purification and Properties of a Nucleoside Triphosphate Pyrophosphohydrolase from Red Cells of the RabbitJournal of Biological Chemistry, 1969
- Separation of deoxyribonucleotides from ribonucleotides by paper chromatographyAnalytical Biochemistry, 1968
- Purification and Some Properties of Inorganic Pyrophosphatase from Human ErythrocytesJournal of Biological Chemistry, 1967
- Effect of Heat and Nucleotides on Human Erythrocyte Inorganic Pyrophosphatase.Experimental Biology and Medicine, 1967
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934