Literature DB >> 24234903

The frequency-domain method reveals the dimeric structure of Na,K-ATPase.

E Amler1, R Staffolani, A Kotyk.   

Abstract

Lucifer yellow and lissamine rhodamine sulfonyl hydrazine were used as the donor and the receptor, respectively, for Förster energy transfer measurements to determine the location of the β subunit in the native Na,K-ATPase from pig kidney. It was found that (1) the β subunits are located in one functional complex, i.e., the dimer (αβ)2 appears to be the functional complex of Na,K-ATPase, and (2) the β subunits in the functional enzyme complex in the membrane are not located next to each other but are rather well separated. The distance between fluorophores covalently attached to the β subunits was found to be 5.3 nm.

Entities:  

Year:  1993        PMID: 24234903     DOI: 10.1007/BF00865271

Source DB:  PubMed          Journal:  J Fluoresc        ISSN: 1053-0509            Impact factor:   2.217


  5 in total

1.  Correction for contaminant fluorescence in frequency-domain fluorometry.

Authors:  J R Lakowicz; R Jayaweera; N Joshi; I Gryczynski
Journal:  Anal Biochem       Date:  1987-02-01       Impact factor: 3.365

2.  Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization.

Authors:  E Haas; E Katchalski-Katzir; I Z Steinberg
Journal:  Biochemistry       Date:  1978-11-14       Impact factor: 3.162

3.  Labeling of the glycoprotein subunit of (Na,K)ATPase with fluorescent probes.

Authors:  J A Lee; P A Fortes
Journal:  Biochemistry       Date:  1985-01-15       Impact factor: 3.162

4.  Large-scale purification of Na,K-ATPase and its protein subunits from lamb kidney medulla.

Authors:  L K Lane; J D Potter; J H Collins
Journal:  Prep Biochem       Date:  1979

5.  Structural dynamics and oligomeric interactions of Na+,K(+)-ATPase as monitored using fluorescence energy transfer.

Authors:  E Amler; A Abbott; W J Ball
Journal:  Biophys J       Date:  1992-02       Impact factor: 4.033

  5 in total

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