The enzymic hydrolysis of adenosine triphosphate by liver mitochondria. 1. Activities at different pH values

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The enzymic hydrolysis of adenosine triphosphate by liver mitochondria. I. Activities at different pH values.

more toxic by intraperitoneal injection than any of the simple peroxides with which it was compared. Autoxidized methyl linoleate was less toxic than most of the simple peroxides. 5. The LD50 of autoxidized linoleic acid (0.26 ,mole of peroxide/g.) was only slightly higher than the mean increase of peroxide previously found in mice after 950r. of X-rays (0.22 lamole/g.). 6. Injected peroxides k...

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The enzymic hydrolysis of adenosine triphosphate by liver mitochondria. 2. Effect of inhibitors and added cofactors.

Potter, V. R. & Recknagel, R. 0. (1951). In Phosphorus Metaboli8m, vol. 1, p. 377. Ed. by McElroy, W. D. & Glass, B. Baltimore: Johns Hopkins Press. Potter, V. R., Siekevitz, P. & Simonson, H. C. (1953). J. biol. Chem. 205, 893. Robertson, H. E. & Boyer, P. D. (1955). J. biol. Chem. 214, 295. Sacktor, B. (1953). J. gen. Phy8iol. 36, 371. Schneider, W. C. & Hogeboom, G. H. (1950). J. biol. Chem....

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Mechanism of adenosine triphosphate hydrolysis by actomyosin.

The hydrolysis of ATP by acto-HMM has been studied during the transient state using a rapid-mixing apparatus. The rate of substrate binding was slightly slower and the rate of hydrolysis of the first molecule of ATP was essentially the same as for heavy meromyosin (HMM) alone. The rate of acto-HMM dissociation after binding substrate was too fast to measure in a stopped-flow apparatus, conseque...

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The pH-dependence of enzymic ester hydrolysis.

The esterases of animal tissues have generally been characterized by their substrate specificity and by their behaviour towards various inhibitors. The irreversible inhibition by organic phosphates, which is due to phosphorylation of the active group (Burgen, 1949; Wilson & Bergmann, 1950a; Aldridge, 1953d), is a common property of most esterases, an interesting exception being the Aesterase of...

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K+ is required for the stimulation by the antibiotic nigericin of adenosine triphosphate hydrolysis in rat liver mitochondria. This action does not occur when K+ is replaced by other monovalent cations. It requires slightly hypotonic conditions and is not related to the swelling phenomena linked to the accumulation of K+ in mitochondria. ATPase is inhibited by small anion molecules to which the...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1957

ISSN: 0306-3283

DOI: 10.1042/bj0670558