Fluorometric Measurement of Adenosine 5'-Triphosphate Using Exonuclease V Activity
نویسندگان
چکیده
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...
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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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SERUM CREATINE KINASE activity has beell measured by determining the amount of creatine liberated in the following reaction: ADI + creatine phosphate ATP + creatine. The Voges-Proskauer reactioii, production of a color by reaction of creatille with diacetyl alid -naphthol, has heeii used to measure enzymatically released creatine (1-5). The presence of a sulfhydryl compound in tile incubatioii ...
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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: Journal of Photopolymer Science and Technology
سال: 2018
ISSN: 0914-9244,1349-6336
DOI: 10.2494/photopolymer.31.699