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ATPaseAdenosine Triphosphatase
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Ca2+-activated ATPase enzyme (Ca2+-ATPase) activity was determined for samples at different storage time and expressed as micrograms of inorganic phosphorous (Pi) per milligram protein per minute.
The authors noted certain limitations in this study that the multiplicity of nucleotide processing events in distinct ATPases, during transitions between consecutive states of the proteasome, may have resulted in the absence of fast steps and sparsely populated intermediate states in their cryo-EM reconstructions.
Effect of ischemia-reperfusion on Na+, K+- ATPase expression in human liver tissue allograft: image analysis by confocal laser scanning microscopy.
The sensitivity of [Na.sup.+], [K.sup.+] ATPase as an indicator of blood diseases.
Based on the results, the following antibacterial mechanism of BPCE is proposed: BPCE rapidly destroys bacterial cell walls and membranes and decreases the ATPase level.
Hiesinger, "The vesicular ATPase: a missing link between acidification and exocytosis," The Journal of Cell Biology, vol.
Since ATPase activity of [[alpha].sub.3][beta][(E190CmCys).sub.3][gamma] was 12% of that of [[alpha].sub.3][[beta].sub.3][gamma], (30) the role of the carboxylate at the 190 position in the [F.sub.1]-ATPase could be discussed.
Previous studies demonstrated that one of the main mechanisms of nervous impairments was the inhibition of adenosinetriphosphatase (ATPase) activity as well as the increasing intracellular calcium concentration [14-16].
One postulated theory is the effect of thyroid hormone on the cardiac myocyte Na/K1 ATPase. It is proposed that increased activity in this receptor secondary to the action of T4 corresponds with increased intracellular potassium causing hyperpolarization of the membrane and prolonging repolarization represented as a prolonged QTc.
It is located in exon 18, which is part of the major SNF2 ATPase domain of the SMARCA2 gene, specifically in the II helicase-related sequence motif of the Helicase ATP-binding domain [9,13].
The intraluminal space of the endosome and lysosome is acidified by vacuolar-type [H.sup.+] ATPase (V-ATPase) at the endosomal membrane.
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