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.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
L. K. Lane, J. D. Potter, and J. H. Collins (1979)Prep. Biochem. 9, 157–170.
E. Amler, A. Abbott, and W. J. Ball, Jr. (1992)Biophys. J. 61, 553–568
J. A. Lee and P. A. G. Fortes (1985)Biochemistry 24, 322–332.
J. R. Lakowicz, R. Jayaweera, N. Jøshi, and I. Gryczynski (1987)Anal. Biochem. 160, 471–479.
E. Haas, E. Katchalski, and I. Z. Steinberg (1978)Biochemistry 17, 5061–5070.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Amler, E., Staffolani, R. & Kotyk, A. The frequency-domain method reveals the dimeric structure of Na,K-ATPase. J Fluoresc 3, 245–246 (1993). https://doi.org/10.1007/BF00865271
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00865271