Zobrazeno 1 - 10
of 88
pro vyhledávání: '"R, Goldshleger"'
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:
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. 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. 268(5)
The principal objective of this work has been to determine whether Asn831 of the alpha chain of Na/K-ATPase is located at the cytoplasmic or extracellular surface. Asn831 is the N-terminal residue of a 19-kDa C-terminal tryptic fragment which, togeth
Publikováno v:
The Journal of biological chemistry. 267(2)
This paper extends our recent report that renal Na+,K(+)-ATPase is digested by trypsin in the absence of Ca2+ and presence of Rb+ ions to a stable 19-kDa fragment and smaller membrane-embedded fragments of the alpha chain and essentially intact beta
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 607
This paper summarises results and conclusions from experiments with renal Na/K-ATPase, utilising proteolytic digestion to define minimal peptide structures involved in cation occlusion and chemical modification with dicyclohexylcarbodiimide (DCCD) to
Publikováno v:
Society of General Physiologists series. 46