Demonstration of a Mg-ATPase and a Na,K-ATPase from the arteria carotis communis of the sheep.
Besides the Mg-ATPase, a Na,K-ATPase can be demonstrated in different fractions of smooth muscles of the A. carotis communis of the sheep. The highest activity of Mg-ATPase is observed in the heavy microsomal fraction. The Ca-ion may act as a complete substitute for the Mg-ion in the Mg-ATPase. The proportion of Na,K-ATPase is between 10 and 40%, depending on the preparative conditions used in the individual fractions. Fractionated salt treatment (LiBr, KC1, KBr) improved the assay of Na,K-ATPase but increased strength of the Tris-HC1-buffer considerably reduced its activity.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D002339:Carotid Arteries / Q000201:enzymology*; D003579:Cytochrome Reductases / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D008274:Magnesium; D008861:Microsomes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D009130:Muscle, Smooth / Q000201:enzymology; D011188:Potassium; D012756:Sheep / Q000378:metabolism*; D012964:Sodium; D013385:Succinate Dehydrogenase / Q000378:metabolism; D013552:Swine / Q000378:metabolism
D012964:Sodium; D005954:Glucosephosphate Dehydrogenase; D013385:Succinate Dehydrogenase; D003579:Cytochrome Reductases; D001219:Aspartate Aminotransferases; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium