Results 211 to 220 of about 275,929 (264)
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Journal of Biochemistry, 1995
Sliding machines composed of F-actin and myosin or microtubules and kinesin or dynein convert the free energy of ATP hydrolysis into sliding movements and mechanical work. Development of optical microscopy with micromanipulation techniques has made possible direct observation of single events of sliding exhibited by single sliding machines.
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Sliding machines composed of F-actin and myosin or microtubules and kinesin or dynein convert the free energy of ATP hydrolysis into sliding movements and mechanical work. Development of optical microscopy with micromanipulation techniques has made possible direct observation of single events of sliding exhibited by single sliding machines.
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Molecular and Cellular Biochemistry, 1981
An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism.
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An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism.
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Crystals of an ATPase fragment of bovine clathrin uncoating ATPase
Journal of Molecular Biology, 1988A 44,000 Mr amino-terminal, clathrin-independent ATPase fragment of the bovine clathrin uncoating ATPase has been crystallized in a form suitable for X-ray diffraction studies. The crystals are orthorhombic, space group P2(1)2(1)2(1), a = 145.3 A, b = 65.0 A, c = 46.9 A, with one protein molecule per asymmetric unit (1 A = 0.1 nm).
C, DeLuca-Flaherty +4 more
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Regulatory proteins of F1F0-ATPase: Role of ATPase inhibitor
Journal of Bioenergetics and Biomembranes, 1990An intrinsic ATPase inhibitor inhibits the ATP-hydrolyzing activity of mitochondrial F1F0-ATPase and is released from its binding site on the enzyme upon energization of mitochondrial membranes to allow phosphorylation of ADP. The mitochondrial activity to synthesize ATP is not influenced by the absence of the inhibitor protein.
T, Hashimoto, Y, Yoshida, K, Tagawa
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Regulation of Ca2+-ATPases,V-ATPases and F-ATPases
2016The biological membranes of cellular organization enfold an important group of membrane proteins called the ATPases, which are not only versatile in maintaining chemical gradient and electrical potential across the membrane but also bring metabolites necessary for cell metabolism and drive out toxins, waste products and solutes that otherwise can curb ...
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Activation of Mg-ATPase (Spectrin-Dependent ATPase) by Ca^2+
Enzyme, 2017The dependence of saponin-stimulated Mg-ATPase activity in the erythrocyte membrane on Ca^2+ concentration was studied. In the membrane of freshly sampled human erythrocytes we found for this enzyme and Ca2+ an apparent dissociation constant of 0.611 µmol/l (SE ± 0.106 µmol/l) and Hill coefficient of 0.93 (SE ± 0.05).
L, Mircevová +3 more
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The interaction between the mitochondrial ATPase (F1) and the ATPase inhibitor
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 19731. The naturally occurring mitochondrial ATPase inhibitor inhibits the mitochondrial ATPase (F1) non-competitively. 2. The interaction between inhibitor and inhibitor-depleted F1 or submitochondrial particles is diminished when the ratio of ATP/ADP is low or when energy is generated by substrate oxidation. 3.
R J, van de Stadt +2 more
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Nihon rinsho. Japanese journal of clinical medicine, 1997
Gastric H+, K+ -ATPase comprised of alpha- and beta-subunits was functionally expressed in an animal cell-line. When glutamic acid (345) of the alpha-subunit was mutated to glutamine, the affinity of K+ decreased 10-fold, indicating that this residue in the 4th transmembrane domain engages in the determination of the K+ affinity.
N, Takeguchi, S, Asano, M, Morii
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Gastric H+, K+ -ATPase comprised of alpha- and beta-subunits was functionally expressed in an animal cell-line. When glutamic acid (345) of the alpha-subunit was mutated to glutamine, the affinity of K+ decreased 10-fold, indicating that this residue in the 4th transmembrane domain engages in the determination of the K+ affinity.
N, Takeguchi, S, Asano, M, Morii
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The International Journal of Biochemistry & Cell Biology, 2008
The vacuolar H(+)-ATPase (V-ATPase) is a universal component of eukaryotic organisms, which is present in both intracellular compartments and the plasma membrane. In the latter, its proton-pumping action creates the low intravacuolar pH, benefiting many processes such as, membrane trafficking, protein degradation, renal acidification, bone resorption ...
Yong-Tao, Xiao +2 more
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The vacuolar H(+)-ATPase (V-ATPase) is a universal component of eukaryotic organisms, which is present in both intracellular compartments and the plasma membrane. In the latter, its proton-pumping action creates the low intravacuolar pH, benefiting many processes such as, membrane trafficking, protein degradation, renal acidification, bone resorption ...
Yong-Tao, Xiao +2 more
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Journal of Bioenergetics and Biomembranes, 1992
The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of ...
Skou, J C, Esmann, Mikael
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The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of ...
Skou, J C, Esmann, Mikael
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