Results 171 to 180 of about 104,099 (211)

Structure of the Vacuolar Adenosine Triphosphatases

Cell Biochemistry and Biophysics, 2001
Vacuolar adenosine triphosphatases (V-ATPases) represent an important class of proton pumps found in endomembrane systems of eucaryotic cells, where they are involved in pH regulation. Progress has been made in the structure determination of this large, membrane-bound multisubunit enzyme complex.
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Adenosine Triphosphatase Activity of Mycoplasma Membranes

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
S, Rottem, S, Razin
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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
G F, MALEY, D, JOHNSON
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Intermediate states of actomyosin adenosine triphosphatase

Biochemistry, 1976
The early kinetic steps of actomyosin subfragment 1 (acto-S1) adenosine triphosphatase have been investigated by simultaneous monitoring of fluorescence and light scattering and also by observation of the time course of the production of phosphate. The results show that fluorescence enhancement occurs after the dissociation of actomyosin and that the ...
J A, Sleep, E W, Taylor
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Mitochondrial adenosine triphosphatase

Journal of Bioenergetics, 1975
Subuni 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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Adenosine triphosphatase activities in Trypanosoma cruzi

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1978
1. Subcellular fractions obtained from epimastigotes of Trypanosoma cruzi, disrupted by three different procedures, contained in addition to the already known Mg2+-activated adenosine triphosphatase (ATPase; E.C.3.6.1.4), a Ca2+-ATPase activity. 2. The Ca2+-ATPase (a) was activated by low concentrations of CaCl2 (apparent Ka, 80 microM); (b) had a Km ...
A C, Frasch, E L, Segura, J J, Cazzulo, A O, Stoppani   +3 more
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Adenosine triphosphatase of mycobacteria.

Microbios, 1980
A Mg+2-(Ca+2)-activated adenosine triphosphatase activity has been demonstrated in saprophytic, human pathogenic and non-pathogenic, and atypical, species of mycobacteria. (Na+ + K+)-activated adenosine triphosphatase was absent in the species investigated.
G, Grover, K R, Dhariwal, T A, Venkitasubramanian   +2 more
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Molecular kinetics of muscle adenosine triphosphatase

Archives of Biochemistry and Biophysics, 1952
Abstract 1. 1. The kinetics of the dephosphorylation of ATP by myosin follow the law, −d [ ATP ] dt = k 2 K[ myosin ][ ATP ] (1 + K [ ATP ]) . The apparent heats and entropies associated with K2 and K are, respectively, Δ H 2 ‡ = 12.4 kcal, mole −1 ; Δ S 2 ‡ = −8 cal. mole −1
L, OUELLET, K J, LAIDLER, M F, MORALES
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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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The Mitochondrial Adenosine Triphosphatase

1982
In the previous chapter we saw that the ATPase activity of coupled mitochondria is dramatically stimulated by uncouplers and more generally by conditions that interrupt the flow of energy from the electron transfer chain to the coupling device. These observations have for a long time been interpreted to indicate that the ATPase is involved in the ...
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