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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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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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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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Current Opinion in Nephrology and Hypertension, 1997
Na,K-ATPase is the driving force for renal Na+ reabsorption and is thus critically implicated in the control of extracellular volume and blood pressure. This review focuses on most recent advances in the elucidation of intrinsic structural features that are important for Na,K-ATPase function and in the identification of regulatory mechanisms that are ...
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Na,K-ATPase is the driving force for renal Na+ reabsorption and is thus critically implicated in the control of extracellular volume and blood pressure. This review focuses on most recent advances in the elucidation of intrinsic structural features that are important for Na,K-ATPase function and in the identification of regulatory mechanisms that are ...
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Properties of ATPase in chloroplasts
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969Abstract 1. 1. Mg 2+ -ATPase (light-triggered Mg 2+ -dependent ATPase) activity in chloroplasts was stimulated by atebrin, NH 4 Cl and gramicidin when the uncouplers were added after light triggering. The stimulation was followed in time by inhibition when the reaction took place in the dark. 2. 2.
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Journal of Experimental Biology, 1992
ABSTRACT Protons migrate much faster than other ions through water, ice and water-lined membrane channels because they participate in hydrogen bonding and H+H2O exchange. Similarly, hydrogen bonding enables protons with amino, carbonyl, phosphoryl and sulfonyl residues to influence critically the charge, conformation and stability of ...
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ABSTRACT Protons migrate much faster than other ions through water, ice and water-lined membrane channels because they participate in hydrogen bonding and H+H2O exchange. Similarly, hydrogen bonding enables protons with amino, carbonyl, phosphoryl and sulfonyl residues to influence critically the charge, conformation and stability of ...
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Current Biology, 1992
Proton pumps that belong to the families of F-ATPases and V-ATPases operate without the formation of a phosphorylated intermediate and contain several subunits grouped into distinct catalytic and membrane sectors. Recent studies on the structure and molecular biology of V-ATPases shed light not only on the structure-function relations between the two ...
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Proton pumps that belong to the families of F-ATPases and V-ATPases operate without the formation of a phosphorylated intermediate and contain several subunits grouped into distinct catalytic and membrane sectors. Recent studies on the structure and molecular biology of V-ATPases shed light not only on the structure-function relations between the two ...
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1984
Publisher Summary This chapter focuses on one aspect of the biochemistry of mitotic spindles—the presence of adenosine triphosphate (ATP) hydrolyzing enzymes. ATPase in the mitotic spindle is discussed. There is a physiological evidence for dynein ATPase in mitotic spindles.
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Publisher Summary This chapter focuses on one aspect of the biochemistry of mitotic spindles—the presence of adenosine triphosphate (ATP) hydrolyzing enzymes. ATPase in the mitotic spindle is discussed. There is a physiological evidence for dynein ATPase in mitotic spindles.
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