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Энергетика биологических мембран - Скулачев В.П.

Скулачев В.П. Энергетика биологических мембран — М.: Наука, 1989. — 564 c.
ISBN 5-02-004027-4
Скачать (прямая ссылка): energetikabiologicheskihmembran1989.djvu
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1147. Ovchinnikov Yu. A., Abdulaev N. G., Feigina M. Yu., Kiselev A. V.,. Lobanov N. A. The structural basis of the functioning of bacteriorhodopsin: an overview // Ibid. 1979. Vol. 100. P. 219—224.
1148. Ovchinnikov Yu. A., Abdulaev N. G., Kiselev A. V., Drachev L. A.,-Kaulen A. D., Skulachev V. P. The water-exposed C-terminal. seguence of bacteriorhodopsin does not affect H+-pumping // Ibid.
1986. Vol. 194. P. 16-20.
1149. Ovchinnikov Yu. A., Abdulaev N. G., Vasilov R. G., Vturina I. Yu.,-Kuryatov A. B., Kiselev 4. Y.The antigenic structure and topography of bacteriorhodopsin in purple membranes as determined by interaction with monoclonal antibodies // Ibid. 1985. Vol. 179. P. 343—349.
1150. Ovchinnikov Yu. A., Demin V. V., Barnakov A. N., Kuzin A. P., Lunev A. V., Modyanov N.N., Dzhandzhugazyan K.N. Three-dimensional structure of (Na+ + K+)—ATPase revealed by electron microscopy of two-dimensional crystals // Ibid. Vol. 190. P. 73—76.
1151. Ovchinnikov Yu. A., Modyanov N. N., Broude N. , Petrukhin K. E.r Grishin A. V., Arzamazova N. M., A Idanova N. A ., M onastyrskay a G. F
512
Список литературы
Sverdlov Е. D. Pig kidney Na+, K+—ATPase. Primary structure and spatial organization // Ibid. 1986. Vol. 201. P. 237—245.
1152. Ovchinnikov Yu. A . Modyanov N. N., Grinkevich V. A ., A Idanova N. A ., Kostetsky P. V., Trubetskaya О. E., Hundal Т., Ernster L. Oligomycin sensitivity-conferring protein (OSCP) of beef heart mitochondria. Internal sequence homology and structural relationship with other proteins // Ibid. 1984. Vol. 175. P. 109—112.
1153. Ovchinnikov Yu. A ., Modyanov N ? N., Grinkevich V. A., A Idanova N. A ., Trubetskaya О. E., Nazimov I. V., Hundal Т., Ernster L. Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the S-subunit of the Fj—ATPase of Escherichia coli // Ibid. Vol. 166. P. 19—22.
1154. Ozawa T. Mitochondrial electron transport system//Transport and bioenergetics in biomembranes /Ed. R. Sato, Y. Kagawa. Tokyo; N. Y.; L.: Jap. Sci. Soc. press: Tokyo Plenum press, 1982. P. 1—36.
1155. Ozols J., Carr S. A ., Strittmatter P. Identification of the NH2-terminal blocking group of NADH-cytochrome bb reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain // J. Biol. Chem. 1984. Vol. 259. P. 13349—13354.
1156. Packham N. K., Berriman J. A., Jackson J. B. The charging capacitance of the chromatophore membrane // FEBS Lett. 1978. Vol. 89. P. 205—210.
1157. Padan E., Zilberstein D., Schuldiner S. pH homeostasis in bacteria // Biochim. et biophys. acta. 1981. Vol. 650. P. 151—166.
1158. Pages J. MLazdunski С. Maturation of exported proteins in Escherichia coli. Requirement for energy, site and kinetics of processing // Europ. J. Biochem. 1982. Vol. 124. P. 561—566.
1159. Paillotin G., Vermeglio A., Breton J. Orientation of reaction center and antenna chromatophores in the photosynthetic membrane of Rho-dopseudomonas viridis // Biochim. et biophys. acta. 1979. Vol. 545. P. 249-264.
1160. Palacios-Romero R., Mowbray J. Evidence for the rapid control both in vivo and in vitro of the efficiency of oxidative phosphorylation by 3, 5, 3'-tri-iodo-L-thyronine in rats // Biochem. J. 1977. Vol. 184. P. 527—
538.
1161. Pande S. V., Blanchaer M. C. Reversible inhibition of mitochondrial adenosine diphosphate phosphorylation by long chain acyl coenzyme A esters//J. Biol. Chem. 1971. Vol. 246. P. 402—411.
1162. Pande S. V., Parvin R. Characterization of carnitine-acylcarnitine translocase system of heart mitochondria // Ibid. 1976. Vol. 251. P. 6683—6691.
1163. Pande S. V., Parvin R. Carnitine-acylcarnitine translocase catalyzes an equilibrating unidirectional transport as well // Ibid. 1980. Vol. 255. P. 2994—3001.
1164. Panov A., Filippova S., Lyakhovich V. Adenine nucleotide translocase as a site of regulation by ADP of the rat liver mitochondria permeability for H+and K+ions//Arch. Biochem. a. Biophys. 1980. Vol. 199. P. 420—
426.
1165. Panov A. F., Konstantinov Yu. M., Lyakhovich V. V. The possible role of palmitoyl-CoA in the regulation of the adenine nucleotides transport in mitochondria under different metabolic states// J.Bioenerg. Bio-membr. 1975. Vol. 7. P. 75—85.
1166. Papadimitriou A ., Neustein H. В., Dimauro S., Stanton R., Bresolin N. Histiocytoid cardiomyopathy of infancy: deficiency of reducible cytochrome b in heart mitochondria // Pediat. Res. 1984. Vol. 18. P. 1023-1028.
1167. Pappin D. J. С., Eliopoulos E., Brett M., Findlay J. В. С. A structural model for ovine rhodopsin // Intern. J. Biol. Macromol. 1984. Vol. 6. P. 73—76.
Список литературы
513
1168. Paradies Н. Н., Schmidt U. D. Size and molecular parameters of adenosine triphosphatase from Escherichia coli // J. Biol. Chem. 1979. Vol.
254. P. 5257- 5263.
1169. Parson W. W? Photosynthetic bacterial reaction centers: interactions among the bacteriochlorophylls and bacteriopheophytins // Annu. Rev. Biophys. a. Bioenerg. 1982. Vol. 11. P. 57—80.
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