Results 151 to 160 of about 363,756 (199)
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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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Current Opinion in Nephrology and Hypertension, 1999
The H+,K+-ATPases comprise a group of integral membrane proteins that belong to the X+,K+-ATPase subfamily of P-type cation-transporting ATPases. Although these H+,K+-ATPase isoforms share approximately 60-70% amino acid identity, they exhibit discrete kinetic and pharmacological properties when expressed in heterologous systems.
T D, DuBose, J, Gitomer, J, Codina
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The H+,K+-ATPases comprise a group of integral membrane proteins that belong to the X+,K+-ATPase subfamily of P-type cation-transporting ATPases. Although these H+,K+-ATPase isoforms share approximately 60-70% amino acid identity, they exhibit discrete kinetic and pharmacological properties when expressed in heterologous systems.
T D, DuBose, J, Gitomer, J, Codina
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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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2016
The Na+/K+-ATPase is a universally expressed membrane protein responsible for maintaining the low intracellular Na+ and high intracellular K+ concentrations required for multitude of cellular functions. Besides, the Na+ /K+-ATPase helps maintaining resting potential, import of amino acids, glucose, and other nutrients into cells and regulates cellular ...
Obradović, Milan +4 more
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The Na+/K+-ATPase is a universally expressed membrane protein responsible for maintaining the low intracellular Na+ and high intracellular K+ concentrations required for multitude of cellular functions. Besides, the Na+ /K+-ATPase helps maintaining resting potential, import of amino acids, glucose, and other nutrients into cells and regulates cellular ...
Obradović, Milan +4 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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Trends in Biochemical Sciences, 1989
Since the pioneering work of Peter Mitchell 1, the central role of proton gradients in biological energy transduc- tion has been widely ackrLowledged. The enzymes directly involved in generating and harnessing the energy of proton gradients (H+-ATPases), are found in nearly all cells and presumably appeared very early in cell evolution 2.
N, Nelson, L, Taiz
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Since the pioneering work of Peter Mitchell 1, the central role of proton gradients in biological energy transduc- tion has been widely ackrLowledged. The enzymes directly involved in generating and harnessing the energy of proton gradients (H+-ATPases), are found in nearly all cells and presumably appeared very early in cell evolution 2.
N, Nelson, L, Taiz
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Journal of Bioenergetics and Biomembranes, 1981
F1-ATPases are large multimeric proteins that can be isolated from the membrane bound system that catalyzes the phosphorylation of ADP by inorganic phosphate in bacteria, plants, and mitochondria. They can be visualized in electron micrographs of the inner mitochondrial membranes where they appear as large protruding spheres 90 A in diameter.
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F1-ATPases are large multimeric proteins that can be isolated from the membrane bound system that catalyzes the phosphorylation of ADP by inorganic phosphate in bacteria, plants, and mitochondria. They can be visualized in electron micrographs of the inner mitochondrial membranes where they appear as large protruding spheres 90 A in diameter.
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[H(+)-ATPase and H(+), K(+)-ATPase].
Nihon rinsho. Japanese journal of clinical medicine, 1992Two different types of proton transporting ATPases, v-and p-type H(+)-ATPases engage in epithelial ion transport. Properties, function, molecular structure and distribution of these H(+)-ATPase (v-type) and H+, K(+)-ATPase (p-type) are summarized here. Intraorganellar spaces, such as lysosome, synapse, multivesicular body, are acidified by the vacuole ...
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1997
Evidence is presented that brush-border membrane vesicles purified from homogenates of rat kidney cortex posses an ecto-enzyme activity that is responsible for the hydrolysis of both ATP and ADP, as well as for the hydrolysis of other nucleoside tri- and diphosphates.
Griparić, Lorena +1 more
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Evidence is presented that brush-border membrane vesicles purified from homogenates of rat kidney cortex posses an ecto-enzyme activity that is responsible for the hydrolysis of both ATP and ADP, as well as for the hydrolysis of other nucleoside tri- and diphosphates.
Griparić, Lorena +1 more
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