Zobrazeno 1 - 10
of 61
pro vyhledávání: '"A J, Karlish"'
Publikováno v:
Journal of bioenergetics and biomembranes. 33(5)
This chapter describes contributions of transition metal-catalyzed oxidative cleavage of Na+,K+-ATPase to our understanding of structure-function relations. In the presence of ascorbate/H2O2, specific cleavages are catalyzed by the bound metal and be
Publikováno v:
Journal of bioenergetics and biomembranes. 33(5)
This article reviews our studies of the gamma subunit of the sodium pump. Gamma is a member of the FXYD family of small, single transmembrane proteins and is expressed predominantly in the kidney tubule. There are two major variants of gamma which fu
Publikováno v:
The Journal of biological chemistry. 276(51)
In the presence of ascorbate/H(2)O(2), Fe(2+) ions or the ATP-Fe(2+) complex catalyze selective cleavage of the alpha subunit of gastric H(+),K(+)-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E(1)
Publikováno v:
The Journal of biological chemistry. 276(23)
The gamma subunit of the Na,K-ATPase is a member of the FXYD family of type 2 transmembrane proteins that probably function as regulators of ion transport. Rat gamma is present primarily in the kidney as two main splice variants, gamma(a) and gamma(b
Publikováno v:
The Journal of biological chemistry. 275(24)
The gamma subunit is a specific regulator of Na,K-ATPase expressed mainly in kidney. On SDS-polyacryylamide gel electrophoresis, gamma runs as a doublet, but the origin and significance of the doublet is obscure. Mass spectrometry of the gamma chains
Publikováno v:
The Journal of biological chemistry. 275(3)
Based on the following observations we propose that the cytoplasmic loop between trans-membrane segments M6 and M7 (L6/7) of the alpha subunit of Na(+),K(+)-ATPase acts as an entrance port for Na(+) and K(+) ions. 1) In defined conditions chymotrypsi
Publikováno v:
The Journal of biological chemistry. 274(5)
This study characterizes disulfide cross-links between fragments of a well defined tryptic preparation of Na,K-ATPase, 19-kDa membranes solubilized with C12E10 in conditions preserving an intact complex of fragments and Rb occlusion (Or, E., Goldshle
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 643
This paper describes a novel technique for specific cleavage of renal Na/K-ATPase, based on bound transition metal ions. The approach might have application to other P-type pumps or membrane proteins. In one type of experiment, specific cleavages of
Publikováno v:
The Journal of biological chemistry. 269(34)
A fluorescent dye, RH421, has been used to characterize charge movements associated with cation and cardiotonic steroid binding to Na,K-ATPase and to a specifically trypsinized preparation, so-called "19-kDa membranes." A fluorescence decrease induce
Autor:
A, Shainskaya, S J, Karlish
Publikováno v:
The Journal of biological chemistry. 269(14)
Digestion of renal Na/K-ATPase with trypsin, in the presence of rubidium and absence of calcium ions, produces so-called "19-kDa membranes," containing a C-terminal 19-kDa and smaller fragments (8-12 kDa) of the alpha chain, and a beta chain either i