Formation of oriented membrane multilayers of Na/K-ATPase [electronic resource].
- New York, N.Y. : Columbia University, 1982.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Physical Description:
- Pages: 8 : digital, PDF file
- Additional Creators:
- Columbia University
United States. Department of Energy. Office of Scientific and Technical Information
- The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produces ATP-dependent Na/sup +/ and K/sup +/ fluxes when incorporated into phospholipid vesicles. The ultimate goal of this work is to determine its low resolution structure using both X-ray and neutron diffraction. A number of methods were used to impart lamellar stacking order to highly purified pig Na/K-ATPase membranes. Upon partial dehydration, x-ray diffraction from Na/K-ATPase membrane multilayers at 98% relative humidity yielded discrete reflections of 118 A periodicity, diffracting to 1/14.8 A/sup -1/, additionally, continuous diffraction to 1/10 A/sup -1/ was obtained. Subjecting the membrane multilayers to high magnetic fields improved the quality of the lamellar diffraction dramatically. Neutron diffraction studies of the partially dehydrated Na/K-ATPase membrane multilayers detected a mosaic spread of 2/sup 0/ when the samples were subjected to a magnetic field of 5 Tesla perpendicular to the membrane surface; the reflections were narrower than the camera line width; hence, the lattice disorder has also decreased significantly, although only four orders were measured.
- Published through SciTech Connect.
Brookhaven symposium biology 32, Upton, NY, USA, 1 Jun 1982.
Edelman, I.S.; Wallace, B.A.; Schoenborn, B.P.; Knott, R.; Pachence, J.M.
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