Modification of Na+ ,K+ -ATPase with N-[P-(2-benzimidazolyl) phenylImalelraide.
نویسندگان
چکیده
منابع مشابه
H2O2-modification of Na,K-ATPase. Alterations in external Na+ and K+ stimulation of K+ influx.
Studies, at steady state, of the Na,K-ATPase dependent influx of K+ into bovine lenses in organ culture are used to characterize further the H2O2-modification of the Na+ pump. Control lenses display constants for interaction with external Na+ and K+ similar to those obtained for the erythrocyte. H2O2 treatment of the bovine lens leads to total loss of external Na+ stimulation and alteration of ...
متن کاملThe Na,K-ATPase beta 2 subunit is expressed in rat brain and copurifies with Na,K-ATPase activity.
We have used a cloned fusion protein as antigen to generate an antiserum specific for the rat Na,K-ATPase beta 2 subunit. Utilizing this antiserum, we analyzed some of the structural features and tissue distribution of the beta 2 subunit. Treatment of a rat brain microsomal membrane fraction with N-glycanase F revealed that the beta 2 subunit is composed of an approximately 32 kDa core protein ...
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1 A specific and essential role for Na,K-ATPase α3 in neurons co-expressing α1 and α3* Background: Neurons express two Na,K-ATPase isoforms, the ubiquitous α1 and neuron-specific α3. Result: α3 is important for control of membrane potential and is fully responsible for restoration of large [Na + ] i increases. Conclusion: α1 and α3 are required for basal neuronal function, but α3 controls resto...
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Chimeric cDNAs encoding a sarcoplasmiclendoplasmic reticulum Ca-ATPase (SERCA1) and regions of the Na,K-ATPase a-subunit were constructed to seek the minimal region of the a-subunit sufficient for assembly with the Na,K-ATPase @-subunit. cDNAs encoding a chimera and the chicken @-subunit were coexpressed in mammalian cells and assembly was assayed by immune precipitation of the chimeric subunit...
متن کاملUltrastructure of Na,K-transport vesicles reconstituted with purified renal Na,K-ATPase
To study the size and structure of the Na,K-pump molecule, the ultrastructure of phospholipid vesicles was examined after incorporation of purified Na,K-ATPase which catalyzes active coupled transport of Na+ and K+ in a ratio close to 3Na/2K. The vesicles were analyzed by thin sectioning and freeze-fracture electron microscopy after reconstitution with different ratios of Na,K-ATPase protein to...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1980
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)53613-7