Results 201 to 210 of about 187,251 (248)
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The adenosine triphosphatase activity of the meromyosins
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967Abstract 1. 1.|Mg 2+ does not activate the ATPase (ATP phosphohydrolase, EC 3.6.1.3) of actin-heavy meromyosin complex (acto-HMM) at low ionic strength. 2. 2.|The interaction inhibitor heparin, which dissociates actomyosin and inhibits its ATPase activity, also inhibits the ATPase of acto-HMM. 3.
Andras Muhlrad, S. Bosko, N.A. Biró
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American Journal of Enology and Viticulture, 1980
The presence of membrane-bound, potassium/ hydrogen, adenosine triphosphatases in the vegetative and reproductive tissues of grapevines is proposed. The expected role of this enzyme system in the uptake of monovalent metal cations by the roots and the ...
R. Boulton
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The presence of membrane-bound, potassium/ hydrogen, adenosine triphosphatases in the vegetative and reproductive tissues of grapevines is proposed. The expected role of this enzyme system in the uptake of monovalent metal cations by the roots and the ...
R. Boulton
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Diseases of Renal Adenosine Triphosphatase
The American Journal of the Medical Sciences, 1995Most renal transport is a primary or secondary result of the action of one of three membrane bound ion translocating ATPase pumps. The proximal tubule mechanisms for the reabsorption of salt, volume, organic compounds, phosphate, and most bicarbonate reabsorption depend upon the generation and maintenance of a low intracellular sodium concentration by ...
Neil A. Kurtzman +2 more
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Adenosine Triphosphatase Activity of Mycoplasma Membranes [PDF]
Journal of Bacteriology, 1966 Rottem, Shlomo (Hebrew University, Jerusalem, Israel), and Shmuel Razin . Adenosine triphosphatase activity of mycoplasma membranes. J. Bacteriol. 92: 714–722. 1966.—Adenosine triphosphatase activity of Mycoplasma laidlawii, M. gallisepticum , and
Shlomo Rottem, Shmuel Razin
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Adenosine triphosphatase distribution in mammary tissue [PDF]
The Histochemical Journal, 1978 Lactating mammary tissue from farm animals and small mammals was perfusion-fixed, prior to histochemical procedures, in an effort to localize the ouabain-sensitive Na+/K+-stimulated ATPase enzyme with the use of specific inhibitors. Histochemical evidence suggests that the Na+/K+-stimulated ATPase is located predominantly on the cytoplasmic side of the
F. B. P. Wooding, M. P. Johnson
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, 1973
Microsomal fractions from wheat (Triticum vulgare) and oat (Avena sativa) roots were used to study Mg2+ and Ca2+ activated adenosine triphosphatases, their dependence of pH, and how Mg2+ and Ca2+ compete or add in stimulation and inhibition. Wheat
A. Kylin, M. Kähr
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Microsomal fractions from wheat (Triticum vulgare) and oat (Avena sativa) roots were used to study Mg2+ and Ca2+ activated adenosine triphosphatases, their dependence of pH, and how Mg2+ and Ca2+ compete or add in stimulation and inhibition. Wheat
A. Kylin, M. Kähr
semanticscholar +1 more source
HOUSE FLY ADENOSINE TRIPHOSPHATASES AND THEIR INHIBITION BY INSECTICIDAL ORGANOTIN COMPOUNDS.
Journal of Economic Entomology, 1965Adenosine triphosphatases (ATPases) in the female house fly, Musca domestica L., have been investigated in relation to their inhibition by organotins and other compounds.
G. Pieper, J. Casida
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Organization of Oligomycin-Sensitive Adenosine Triphosphatase
Biochemical Society Transactions, 1976superaggregates to an active tetramer of 360000daltons and a slow phase of half-time 15s representing the subsequent dissociation of tetramer to an inactive dimer. When enzyme at the same concentration is mixed with 5m-ATP, only the rapid phase of tetramer production is observed.
S. Mascarello +3 more
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Mitochondrial adenosine triphosphatase
Journal of Bioenergetics, 1975Subuni ts . . . . . . . . . . . . . . . . . . . . . . 250 Number . . . . . . . . . . . . . . . . . . . . . 250 Molecular weight and s to ich iomet ry . . . . . . . . . . . . . 251 Isola t ion and amino acid compos i t ion . . . . . . . . . . . . 252 Impuri t ies or products o f proteolysis . . . . . . . . . . . . . 255 Biogenesis . . . . . . . . . . . .
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Azasteroids and heart adenosine triphosphatase
Biochemical Pharmacology, 1966Abstract Azasteroids, some known to be active, others to be inactive as inotropic and antishock agents, were tested as inhibitors of a metal-stimulated heart ATPase. In every instance the biologically active azasteroids inhibited catalysis just as did ouabain and the erythrophleum alkaloids.
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