Na+-K+-ATPase in vascular smooth muscle.
Na+-K+-ATPase has been isolated and characterized from canine aortic tissue. The ouabain-sensitive enzyme activity was 24 mumol X mg protein-1 X h-1, and the remaining Mg2+-ATPase activity was 54 mumol X mg protein-1 X h-1. The ratio of Na+-K+-ATPase to ouabain-sensitive K+-phosphatase was 13 to 1, similar to other more homogeneous preparations from other tissues. The dissociation characteristics of the enzyme-glycoside complex of this aortic preparation were the same as for cardiac preparations in that it was stabilized by K+. These data suggest that the nature of both the ATP hydrolytic site of Na+-K+-ATPase and the ouabain binding site are the same in preparations from vascular smooth muscle as in preparations from other tissues.
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors; D000818:Animals; D001011:Aorta; D004285:Dogs; D005260:Female; D006973:Hypertension / Q000201:enzymology; D008274:Magnesium / Q000378:metabolism; D008297:Male; D009131:Muscle, Smooth, Vascular / Q000201:enzymology*; D010042:Ouabain / Q000494:pharmacology; D012964:Sodium / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013997:Time Factors
D010042:Ouabain; D012964:Sodium; D000469:Alkaline Phosphatase; D000254:Sodium-Potassium-Exchanging ATPase; D008274:Magnesium