Na,K-, Mg- and HCO3-adenosine triphosphatases in the rabbit brain choroid plexus.
Properties of adenosine triphosphatases (ATPases) in the choroid plexus of rabbit cerebral ventricles were investigated using tissue homogenates and subcellular fractions. Na,K-ATPase or HCO3-ATPase activity of choroid plexus was significantly lower than that of the brain or the kidney, respectively. Among the homogenates of choroid plexus from the lateral, third and fourth ventricles, there were no differences in the activities of Na,K-, Mg- and HCO3-ATPases. In the choroid plexus, Na,K-ATPase activity was demonstrated to be highest in 10,000 X g fraction, while the highest Mg- and HCO3-ATPase activities were observed in 8,000 X g fraction, the so-called mitochondrial fraction. Ion requirement, pH optimum and ouabain sensitivity of Na,K-ATPase in 10,000 X g fraction of choroid plexus were similar to findings in erythrocytes, brain and kidney. However, properties of Mg- and HCO3-ATPases in 8,000 X g fraction were considerably different from those found in the brain and gastric mucosa. In the choroid plexus, thiocyanate ion inhibited Mg-ATPase as well as HCO3-ATPase. These results indicate that characteristics of ATPase systems in the choroid plexus are to some extent different from those in tissues such as brain, kidney and gastric mucosa.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D001639:Bicarbonates / Q000378:metabolism; D002831:Choroid Plexus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D013861:Thiocyanates / Q000494:pharmacology
D001639:Bicarbonates; D013861:Thiocyanates; D000251:Adenosine Triphosphatases; D000254:Sodium-Potassium-Exchanging ATPase; D008274:Magnesium