Results 161 to 170 of about 261,336 (211)
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Actomyosin ATPase. II. Fiber typing by histochemical ATPase reaction
Muscle & Nerve, 1980AbstractA new method for fiber typing based on staining for actomyosin Ca, Mg‐ATPase is presented. Inclusion of ethanol in the medium enhanced the differentiation of type 2A and 2B fibers. With this technique, type 1, 2A, and 2B fibers can be distinguished in a single‐step procedure for human biopsy samples.
K, Mabuchi, F A, Sréter
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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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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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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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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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[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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2021
The AAA (ATPases associated with diverse cellular activities) protein family encompasses a large group of enzymes in all domains of life. AAA proteins assemble into oligomeric rings and undergo conformational changes during nucleotide hydrolysis cycles, exerted by highly conserved ATPase modules.
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The AAA (ATPases associated with diverse cellular activities) protein family encompasses a large group of enzymes in all domains of life. AAA proteins assemble into oligomeric rings and undergo conformational changes during nucleotide hydrolysis cycles, exerted by highly conserved ATPase modules.
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