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大鼠空肠基底外侧膜中哇巴因不敏感的钠-ATP酶活性

Ouabain-insensitive Na-ATPase activity in the basolateral membrane from rat jejunum.

作者信息

Orsenigo M N, Tosco M, Esposito G, Faelli A

机构信息

Dipartimento di Fisiologia e Biochimica Generali, Universita' di Milano, Italy.

出版信息

Int J Biochem. 1988;20(12):1411-5. doi: 10.1016/s0020-711x(98)90010-6.

Abstract
  1. In the basolateral membrane preparation of the rat enterocyte (jejunal tract) there is not only the well-known (Na,K)-ATPase activity, but also a ouabain-insensitive Na-ATPase. 2. The Na-ATPase is not activated by anions or other monovalent cations. As a substrate, ATP cannot be replaced by other nucleotides. 3. The Na-ATPase is insensitive to ouabain and bumetanide, inhibited partially by furosemide and totally by ethacrynate. 4. The activation of Na-ATPase at different Na concentrations shows an hyperbolic curve (Km = 15.7 +/- 2.3 mM and Vmax = 204 +/- 19 nmoles Pi/mg protein per min) different from the sigmoidal curve (Km = 9.8 +/- 1.2 mM and Vmax = 640 +/- 15 nmoles Pi/mg protein per min) shown by (Na,K)-ATPase. 5. These results are compared with the corresponding ones found in other animals and tissues in which the Na-ATPase was found. 6. The Na-ATPase activity can be interpreted as the enzymatic correspondent of a ouabain-insensitive Na pump, present in the basolateral membrane of the enterocyte different in behaviour with respect to the known Na pump.
摘要
  1. 在大鼠肠上皮细胞(空肠段)的基底外侧膜制剂中,不仅存在众所周知的(钠,钾)-ATP酶活性,还存在一种哇巴因不敏感的钠-ATP酶。2. 钠-ATP酶不会被阴离子或其他单价阳离子激活。作为底物,ATP不能被其他核苷酸替代。3. 钠-ATP酶对哇巴因和布美他尼不敏感,部分被呋塞米抑制,完全被依他尼酸抑制。4. 在不同钠浓度下钠-ATP酶的激活呈现双曲线(Km = 15.7 +/- 2.3 mM,Vmax = 204 +/- 19 纳摩尔无机磷/毫克蛋白质每分钟),这与(钠,钾)-ATP酶呈现的S形曲线(Km = 9.8 +/- 1.2 mM,Vmax = 640 +/- 15 纳摩尔无机磷/毫克蛋白质每分钟)不同。5. 将这些结果与在发现钠-ATP酶的其他动物和组织中发现的相应结果进行比较。6. 钠-ATP酶活性可被解释为存在于肠上皮细胞基底外侧膜中的一种哇巴因不敏感钠泵的酶对应物,其行为与已知钠泵不同。

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