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KMID : 0365819710110010129
Journal of Pusan Medical College
1971 Volume.11 No. 1 p.129 ~ p.138
Studies on the Cell Debris ATPase Activity of the Rat Kidney


Abstract
The activities of Mg activated and Na-K activated ATPase of cell debris fraction from rat kidney was measured in vitro under the variety of conditions.
The effects of temperature, change in osmolality with several solutes (sucrose, dextrose and urea) and inhibitors of sodium transport or metabolism such as ouabain, oligomycin, sodium azide, DNP, furosemide, and acetazolamide on the activities of both ATPase was investigated and the results were summarized as follows.
1. The activity of the Na-K activated ATPase from the cell debris fraction increased as the concentration of protein increases, but the activity of the Na-K activated ATPase per mg protein remained constant.
2. Lowering incubation temperature depressed markedly the activities of both ATPase.
3. Sucrose depressed Na-K ATPase activity whereas dextrose and urea depressed Mg ATPase activity.
4. Ouabain and oligomycin depressed Na-K ATPase activity, however ouabain induced inhibition of Na-K ATPase activity was partially reversed by increasing the potassium concentration, but not that produced by oligomycin.
5. Solium azide and DNP had no effect on Na-K ATPase activity, while sodium azide inhibited Mg
ATPase activity and DNP slightly activated Mg ATPase activity.
6. Furosemide markedly inhibited both Mg- and Na-K ATPase activities while acetazolamide had no
effect on both Mg- and Na-K ATPase activities.
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