Petzold F, Kolb F E
Arch Exp Veterinarmed. 1976;30(3):365-78.
Studies into the activity of adenosine triphosphatase (ATPase) in homogenates of liver, cerebral cortex, renal cortex, and mucosa of small intestine of swine have shown differentiated activity patterns, with peak activity developing in the liver. This has been related to a particularly high metabolism performance of the liver in fattening pigs. No difference was found to exist between magnesium activation of ATPase of swine tissue homogenates and that in tissue obtained from ruminants. ATPase which could be activated by sodium and potassium ions and inhibited by ouabain was detectable from cerebral and renal cortex. Sodium and potassium ATPases accounts from some 25 per cent of the total activity. ATPase that could be stimulated by calcium ions was recorded only from liver homogenate. The optimum pH values of ATPase were between 7.5 and 8 in the liver, 9 in mucosa of small intestine, and 9.5 in cerebral and renal cortex.
对猪的肝脏、大脑皮层、肾皮质和小肠黏膜匀浆中三磷酸腺苷酶(ATP酶)活性的研究显示出不同的活性模式,其中肝脏中的活性最高。这与育肥猪肝脏特别高的代谢性能有关。未发现猪组织匀浆中ATP酶的镁激活与反刍动物组织中的镁激活存在差异。可被钠和钾离子激活并被哇巴因抑制的ATP酶可在大脑和肾皮质中检测到。钠钾ATP酶约占总活性的25%。仅在肝脏匀浆中记录到可被钙离子刺激的ATP酶。肝脏中ATP酶的最佳pH值在7.5至8之间,小肠黏膜中为9,大脑和肾皮质中为9.5。