The Enzymatic Activity and Inhibition of Adenosine 5′-Triphosphate-Creatine Transphosphorylase
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چکیده
منابع مشابه
The enzymatic activity and inhibition of adenosine 5'-triphosphate-creatine transphosphorylase.
From our earlier rate measurements (l), it was not possible to develop a satisfactory kinetic scheme accounting for the dependence of reaction rate on the concentration of certain ions, such as Mg++ and Hf. Recently, however, we have found (2) that some of the anions which we were inadvertently introducing in the earlier work (e.g. in varying the concentration of Mg++ with the use of magnesium ...
متن کاملStudies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase.
Some of the physical and chemical properties of crystalline adenosine triphosphate-creatine transphosphorylase from rabbit muscle (1) have been previously described (2). In 1956, Friedberg reported on the amino acid composition of this enzyme (3). His data, however, were derived from analyses of only two samples hydrolyzed for the same time interval. Preliminary amino acid analyses from this la...
متن کاملKinetic properties and equilibrium constant of the adenosine triphosphate-creatine transphosphorylase-catalyzed reaction.
catalyzed by adenosine triphosphate-creatine transphosphorylase can be described by a reasonable kinetic scheme. It was shown that MgATPzis the “true substrate,” that the Michaelis constant is the dissociation constant of the enzyme-substrate complex, and that the pH-activity curve resembles a single ionization curve with pK N 6.5. It was of interest to study the kinetics of the reverse process...
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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 کاملAdenylate kinase inhibition by adenosine 5'-monophosphate and fluoride in the determination of creatine kinase activity.
The current methods for the determination of creatine kinase (EC 2.7.3.2) activity are derived from Oliver's method, in which AMP is used to decrease interference by adenylate kinase (EC 2.7.4.3). Recently, Szasz et al. and Rosano et al. described methods in which diadenosine pentaphosphate and fluoride, respectively, are used to reduce this interference. However, diadenosine pentaphosphate doe...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1960
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)64548-x