用针对糖蛋白亚基的抗体对棘鲨直肠腺纯化的钠钾激活三磷酸腺苷酶的抑制作用 - Suppr

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超能文献

Inhibition of the purified sodium-potassium activated adenosinetriphosphatase from the rectal gland of Squalus acanthias by antibody against the glycoprotein subunit.

作者信息

Rhee H M, Hokin L E

出版信息

Biochem Biophys Res Commun. 1975 Apr 21;63(4):1139-45. doi: 10.1016/0006-291x(75)90687-7.

DOI:10.1016/0006-291x(75)90687-7

PMID:124172

Abstract

摘要

相似文献

Inhibition of the purified sodium-potassium activated adenosinetriphosphatase from the rectal gland of Squalus acanthias by antibody against the glycoprotein subunit.用针对糖蛋白亚基的抗体对棘鲨直肠腺纯化的钠钾激活三磷酸腺苷酶的抑制作用

Biochem Biophys Res Commun. 1975 Apr 21;63(4):1139-45. doi: 10.1016/0006-291x(75)90687-7.

Molecular properties of purified (sodium + potassium)-activated adenosine triphosphatases and their subunits from the rectal gland of Squalus acanthias and the electric organ of Electrophorus electricus.来自棘鲨直肠腺和电鳗电器官的纯化（钠+钾）激活的三磷酸腺苷酶及其亚基的分子特性。

J Biol Chem. 1975 Jun 10;250(11):4178-84.

Purification and properties of the sodium-potassium transport adenosinetriphosphatase from the rectal gland of the spiny dogfish Squalus acanthias.

J Supramol Struct. 1973;1(4):336-47. doi: 10.1002/jss.400010409.

Purification and properties of the (sodium + potassium)-activated adenosinetriphosphatase and reconstitution of sodium transport.（钠+钾）激活的三磷酸腺苷酶的纯化与性质及钠转运的重建

Ann N Y Acad Sci. 1974;242(0):12-23. doi: 10.1111/j.1749-6632.1974.tb19075.x.

Studies on the characterization of the sodium-potassium transport adenosinetriphosphatase. Nuclear magnetic resonance studies of 23Na binding to the purified and partially purified enzyme.

Arch Biochem Biophys. 1974 Jun;162(2):421-5. doi: 10.1016/0003-9861(74)90200-8.

A simple procedure for the preparation of highly purified (sodium + potassium) adenosinetriphosphatase from the rectal salt gland of Squalus acanthias and the electric organ of Electrophorus electricus.一种从棘鲨直肠盐腺和电鳗电器官中制备高纯度（钠+钾）三磷酸腺苷酶的简单方法。

Anal Biochem. 1978 Jun 1;86(2):378-85. doi: 10.1016/0003-2697(78)90761-3.

Studies on the characterization of the sodium-potassium transport adenosinetriphosphatase. XI. Comparison of kinetic properties of the purified with the impure membrane-bound enzyme from Squalus acanthias.钠钾转运三磷酸腺苷酶的特性研究。XI. 棘鲨纯化的与非纯化的膜结合酶动力学特性的比较。

Arch Biochem Biophys. 1973 May;156(1):342-9. doi: 10.1016/0003-9861(73)90373-1.

Binding of ATP to Na+, K+-ATPase.ATP与钠钾ATP酶的结合。

Ann N Y Acad Sci. 1974;242(0):158-67. doi: 10.1111/j.1749-6632.1974.tb19088.x.

Effects of wheat germ agglutinin and concanavalin A on parameters of highly purified sodium-potassium adenosine triphosphatases from Squalus acanthias and Electrophorus electricus.麦胚凝集素和伴刀豆球蛋白A对来自棘鲛和电鳗的高度纯化的钠钾腺苷三磷酸酶参数的影响。

Biochim Biophys Acta. 1978 Aug 7;525(2):446-54. doi: 10.1016/0005-2744(78)90241-3.

Inhibition of ouabain-binding to (Na+ + K+)ATPase by antibody against the catalytic subunit but not by antibody against the glycoprotein subunit.

Biochim Biophys Acta. 1979 Nov 16;558(1):108-12. doi: 10.1016/0005-2736(79)90319-5.

引用本文的文献

Recognition of sodium- and potassium-dependent adenosine triphosphatase in organs of the mouse by means of a monoclonal antibody.利用单克隆抗体识别小鼠器官中钠钾依赖的三磷酸腺苷酶。

Cell Tissue Res. 1983;234(3):619-32. doi: 10.1007/BF00218655.

Reconstitution of "carriers" in artificial membranes.人工膜中“载体”的重构。

J Membr Biol. 1981;60(2):77-93. doi: 10.1007/BF01870412.

Lack of immunological cross reactivity between the transport enzymes (Na+ + K+)-ATPase and (K+ + H+)-ATPase.

J Bioenerg Biomembr. 1984 Jun;16(3):223-32. doi: 10.1007/BF00751051.

Conformational changes of membrane-bound (Na+--K+)-ATPase as revealed by trypsin digestion.胰蛋白酶消化揭示的膜结合型（Na⁺ - K⁺）-ATP酶的构象变化

J Membr Biol. 1979 Jun 29;48(1):69-94. doi: 10.1007/BF01869257.

Characteristics of antibody inhibition of rat kidney (Na+ -K+)-ATPase.大鼠肾脏（钠钾）-ATP酶的抗体抑制特性

J Membr Biol. 1978 Dec 8;44(1):85-102. doi: 10.1007/BF01940575.

Inhibition of renal (Na+K+)-ATPase and cation transport by an antibody against NaI extracted kidney plasma membranes.

Pflugers Arch. 1977 Sep 16;370(3):269-76. doi: 10.1007/BF00585537.

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