Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.1 (Mg2+-ATPase)
1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The article deals with the influence of sodium dodensylsulfate, lubrol and also of inhibition of Na+,K+-ATPase and Mg2+-ATPase activities by N-ethyl malemid on the form of curves of erythrocyte membranes amperometric titration by Ag+. It is shown that changes in a conformational structure of proteins membranes under the influence of detergents results in the transformation of SH-group of type I to SH-groups of type II. A 70% fall of Na+,K+-ATPase activity has the same result. So, the form of the curves for titration of erythrocyte membranes sulphydryl groups may serve as an indicator to the morpholocial and functional state of the membranes protein part.
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PMID:[Influence of detergents and inhibition of Na+,K+-ATPase and Mg2+ATPase on erythrocyte membrane SH-groups]. 14 2

A number of metals were examined for inhibition of a canine renal calcium, magnesium-activated adenosinetriphosphatase (Ca2+, Mg2+-ATPase). Of the 27 metals investigated, only compounds of mercury, silver, gold, and uranium demonstrated 50% inhibition of the enzyme at concentrations lower than 10(-4) M. The order of inhibitory potency was Hg greater than Ag greater than U greater than Au. Organic mercury (chlormerodrin, mersalyl, p-chloromercuribenzoate) was less potent than inorganic mercuric chloride, but organic gold sodium thiomalate was equipotent with inorganic gold chloride. The inhibition produced by each metal decreased parallel to the decrease in enzyme activity, seen as the source of enzyme moved from the outer cortex inward to the papilla of the kidney. The regions of highest activity showed the greatest inhibition by each metal, and inhibition decreased as the control activity of the tissue decreased. This variability of inhibition was not related to the protein content of the enzyme preparation. As the ATP concentration increased, the inhibition produced by U was reduced; if the Mg (but not the Ca concentration) was increased while the ATP concentration remained constant, the inhibition increased. Changes in the Ca, Mg, and ATP concentrations did not alter the inhibition produced by Hg, Ag, and Au.
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PMID:Inhibition by metals of a canine renal calcium, magnesium-activated adenosinetriphosphatase. 611 68

High-purity viable cells with low mitochondria (pavement cells) and mitochondria-rich content (chloride cells) were successfully isolated from the gill epithelium of Japanese eels, using three-step Percoll gradient low-speed centrifugation. Cytochemistry (silver staining for chloride, rhodamine-123, and Mitotracker for mitochondria and actin/spectrin immunofluorescence) and scanning electron microscope images were used to identify the cell types in the gill epithelium of the eel. Pavement cells were isolated at 97 and 98% purity for freshwater- and seawater-adapted eels, respectively, and chloride cells were obtained at 89 and 92% purity. The enzymatic activities of the isolated cells were determined. Na+-K+-ATPase, Mg2+-ATPase, and succinate dehydrogenase were found mainly in the chloride cell. Alkaline Ca2+-ATPase and low- and high-affinity Ca2+-ATPase were about twice as high in the chloride cell compared with the pavement cell. Transfer of eels to seawater resulted in enlargement of chloride cell sizes and significant increases in Na+-K+-ATPase, Mg2+-ATPase, and succinate dehydrogenase activities, while all Ca2+-ATPases declined by approximately 60-80%. This is the first report demonstrating the successful isolation of freshwater chloride cells and also an exclusive method of getting high-purity seawater chloride cells. The isolated cells are viable and suitable for further cytological and molecular studies to elucidate the mechanisms of ionic transport.
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PMID:Isolation of viable cell types from the gill epithelium of Japanese eel Anguilla japonica. 995 Sep 13