منابع مشابه
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...
متن کاملAdenosine 5'-triphosphate sulphurylase from Saccharomyces cerevisiae.
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. ...
متن کاملAntidipsogenic effects of central adenosine-5'-triphosphate.
Besides other physiological functions, adenosine-5'-triphosphate (ATP) is also a neurotransmitter that acts on purinergic receptors. In spite of the presence of purinergic receptors in forebrain areas involved with fluid-electrolyte balance, the effect of ATP on water intake has not been investigated. Therefore, we studied the effects of intracerebroventricular (icv) injections of ATP (100, 200...
متن کاملComparison of the Metal Ion Promoted Dephosphorylation of Adenosine 5'-triphosphate and Uridine 5'-triphosphate
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...
متن کاملThermodynamics of the hydrolysis of adenosine 5'-triphosphate to adenosine 5'-diphosphate.
The enthalpy of hydrolysis of the enzyme-catalyzed (heavy meromyosin) conversion of adenosine 5'-triphosphate (ATP) to adenosine 5'-diphosphate (ADP) and inorganic phosphate has been investigated using heat-conduction microcalorimetry. Enthalpies of reaction were measured as a function of ionic strength (0.05-0.66 mol kg-1), pH (6.4-8.8), and temperature (25-37 degrees C) in Tris/HCl buffer. Th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44282-8