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
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Inhibition by Adenosine 5'-Triphosphate
Two major species of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) differing in size, pyridine nucleotide specificity, and susceptibility to inhibition by adenosine 5'-triphosphate (ATP) were detected in extracts of Pseudomonas multivorans (which has recently been shown to be synonymous with the species Pseudomonas cepacia) ATCC 17616. The large species (molecular weight ca. 230,000) was acti...
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Transport systems involved in uptake and biliary secretion of bile salts have been extensively studied in rat liver; however, little is known about these systems in the human liver. In this study, we investigated taurocholate (TC) transport in canalicular and basolateral plasma membrane vesicles isolated from 15 human livers (donor age 6-64 yr). ATP stimulated the uptake ofTC into both canalicu...
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1. ATP sulphurylase from Saccharomyces cerevisiae was purified 140-fold by using heat treatment, DEAE-cellulose chromatography and Sepharose 6B gel filtration. 2. The enzyme was stable at -15 degrees C, optimum reaction velocity was between pH7.0 and 9.0, and the activation energy was 62kJ/mol (14.7kcal/mol). 3. The substrate was shown to be the MgATP(2-) complex, free ATP being inhibitory. 4. ...
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Factors affecting inhibition of myosin ATPase by ATP, such as concentration of the enzyme, of ATP, and of the divalent metals, calcium and magnesium, have been studied and the results are reported here. Experiments were carried out under conditions in which no known magnesium effects occurred, so that only the effect of calcium on the nucleoside triphosphatase activity of myosin A could be qual...
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The dephosphorylation of ATP and UTP in dependence on pH proceeds for both nucleoside 5'-triphosphates (NTP) with the same rate indicating that the nucleic base moieties have no influence on this reaction. This is different in the presence of Cu2+ which promotes the scission of the terminal y phosphate group with both NTP5, but with ATP the reaction is considerably more facilitated. Evidence is...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1978
ISSN: 0264-6021
DOI: 10.1042/bj1710817