Formation of oriented membrane multilayers of Na/K-ATPase

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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 ... continued below

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Pages: 8

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Pachence, J.M.; Knott, R.; Edelman, I.S.; Schoenborn, B.P. & Wallace, B.A. January 1, 1982.

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Description

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.

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Pages: 8

Notes

NTIS, PC A02/MF A01.

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  • Brookhaven symposium biology 32, Upton, NY, USA, 1 Jun 1982

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  • Other: DE84006544
  • Report No.: BNL-34143
  • Report No.: CONF-8206240-2
  • Grant Number: AC02-76CH00016
  • Office of Scientific & Technical Information Report Number: 5234537
  • Archival Resource Key: ark:/67531/metadc1065517

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Office of Scientific & Technical Information Technical Reports

Reports, articles and other documents harvested from the Office of Scientific and Technical Information.

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  • January 1, 1982

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  • Feb. 4, 2018, 10:51 a.m.

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  • March 29, 2018, 12:58 p.m.

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Pachence, J.M.; Knott, R.; Edelman, I.S.; Schoenborn, B.P. & Wallace, B.A. Formation of oriented membrane multilayers of Na/K-ATPase, article, January 1, 1982; United States. (digital.library.unt.edu/ark:/67531/metadc1065517/: accessed May 26, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.