Results 241 to 250 of about 17,343 (255)

Membrane Adenosine Triphosphatases of Prokaryotic Cells

Annual Review of Biochemistry, 1979
PERSPECTIVES AND SUMMARY . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . ... . . . . . . . . . . . . . . . INTRODUCTION . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
J. Allan Downie, Graeme B. Cox, Frank Gibson   +2 more
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Kinetics of muscle adenosine triphosphatase

1955
Abstract not available.
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Histochemical adenosine triphosphatase in the subcommissural organ

Experientia, 1963
Die Aktivitat der Adenosintriphosphatase im Subkommissuralorgan wurde mit der histochemischen Methode vonPadykula undHermann3 untersucht. Die Enzymaktivitat konnte bei der Ratte nur in den Ependymzellen und in den Wanden der Kapillaren beobachtet werden. Bei der Kuh zeigten auch die hypendymalen Rosetten und Gange eine deutliche Aktivitat.
S. Talanti, A. Eisalo
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[63] Adenosine triphosphatase: Bacterial

1971
Publisher Summary The membrane fragments prepared from a variety of photosynthetic bacteria, when illuminated, can synthesize adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate (P i ). Chromatophores prepared from the facultative photoheterotroph, Rhodospirillum rubrum , catalyze the hydrolysis of ATP into ADP ...
Y. Horiuti, K. Nishikawa, Takekazu Horio
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Adenosine triphosphatase and morphological integrity of mitochondria

Biochimica et Biophysica Acta, 1957
Abstract Gramicidin, antimycin A, dinitrophenol, and butyl-3,5-diiodo-4-hydroxybenzoate stimulate mitochondrial ATPase at 23° without causing swelling of these particles. Desoxycholate, saponin, and triiodothyroacetic acid activate ATPase at 23° but also produce swelling or rupturing of the mitochondria. Triiodothyronine, thyroxine, stearic acid, and
Diane Johnson, Gladys Feldott Maley
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Model Reaction for Mitochondrial Adenosine Triphosphatase

Nature, 1968
THE soluble adenosine triphosphatase (ATPase) from mitochondria1–3 is activated by several bivalent metal ions, and the pattern of activation is essentially the same whether the enzyme is acting on ATP (Fig. 1) or ITP (Fig. 2). It is clear that the ionic radius is the chief factor determining the ability of a bivalent ion to activate this enzyme.
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Cytochemical Adenosine Triphosphatase of Vorticellid Myonemes

Science, 1960
A highly specific adenosine triphosphatase has been found to be localized in the contractile apparatus of vorticellids. It is most prominent in the cilia as well as in the myonemes which course the latitudes and longitudes of the cell and spiral in the flat peristome.
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The activation of mitochondrial adenosine triphosphatase by calcium

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
Summary 1. The activation of mitochondrial adenosine triphosphatase (EC 3.6.1.4) by Ca2+ was studied using membranes from deoxycholate-disrupted rat-liver mitochondria as the source of enzyme. With. 3 mM ATP and 1–12 mM Ca2+, pH-activity curves in the range of pH 7.4 to 10.0 showed a broad optimum between 8.0 and 9.0. 2.
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An automated adenosine triphosphatase assay

Analytical Biochemistry, 1975
A.J. Thomson, A.D. Dale, A. Youngson
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The Adenosine Triphosphatase Complex of Mitochondria

1976
In eucaryotic organisms, the bulk of cellular ATP is synthesized by a complex process known as oxidative phosphorylation. In procaryotes this is not always the case. While some bacteria are capable of oxidative phosphorylation, others lack this ability and are dependent on ATP produced from glycolysis.
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