Энергетика биологических мембран - Скулачев В.П.
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1280. Ruby E. G., McCabe J. B. An ATP transport system in the intracellular bacterium, Bdellovibrio bacteriovorus 109J //I. Bacteriol. 1986. Vol. 167. P. 1066—1070.
1281. Rudzinska M. A., D’A lecsandro P. A., Trager W. The fine structure of Leishmania donovani and the role of the kinetoplast in the Leishma-nia-septomonadtransformation // I. Protozool. 1964. Vol. 11. P. 166—191.
1282. Runswick M. J., Walker J. E. The amino acid sequence of the P-subu-nits of ATP synthase from bovine heart mitochondria II J. Biol. Chem.
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1282а. Russel J. Т. ДрН, Н~ diffusion potentials and Mg2+—ATPase in neurosecretory vesicles isolated from bovine neurohypophysss // Ibid. 1984. Vol. 259. P. 9496—9507.
1282b. Russel J. T., Holz R. W. Measurement of ДрН and membrane potential in isolated neurosecretory vesicles from bovine neurohypophyses // Ibid. 1981. Vol. 256. P. 5950—5953.
1283. RydstromJ., Lee С.-P., Ernster L. Energy-linked nicotinamide nucleotide transhydrogenase // Chemiosmotic proton circuits in biological membranes / Ed. V. P. Skulachev, P. C. Hinkle L.: Addison-Wesley,
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1284. Rydstrom /., PerssonB., Tang H -I. Mitochondrial nicotinamide nucleotide transhydrogenase // Bioenergetics / Ed. L. Ernster. Amsterdam: Elsevier, 1984. P. 207—219.
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1286. Sachs G., Koelz H. R., Berglindh T., Rabon E., Saccomani G. Aspects of gastric proton-transport ATPase // Membranes and transport / Ed.
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1287. Sackmann E., Trauble H. Studies of the crystalline-liquid crystalline phase transition of lipid model membranes.I. Use of spin labels and optical probes as indicators of the phase transition // J. Amer. Chem. Soc. 1972a. Vol. 94. P. 4482—4491.
1288. Sackmann E., Trauble H? Studies of crystalline-liquid crystalline phase transition ofj lipid model membranes. II. Analysis of electron spin resonance spectra of steroid labels incorporated into lipid membranes // Ibid. 1972b. Vol. 94. P. 4492—4498.
1289. Saermark Т., Flint N., Evans W. H. Hepatic endosome fractions contain an АТР-driven proton pump // Biochem. J. 1985. Vol. 225. P. 51—58.
1290. Saier M. H. The bacterial phosphotransferase system in regulation of carbohydrate permease synthesis and activity // Membranes and transport / Ed. A. N. Martonosi. N. Y.; L.: Plenum press, 1982. Vol. 2. P. 27—32.
1291. Sakamoto J. Effect of dimethylsulfoxide on ATP synthesis by mitochondrial soluble F]— ATPase // J. Biochem. 1984. Vol. 96. P. 483—487.
1292. Sakamoto J., Tonomura Y. Synthesis of enzyme-bound ATP by mitochondrial soluble Fx—ATPase in the presence of dimethylsulfoxide // Ibid. 1983. Vol. 93. P. 1601-1614.
1293. Salamma F. R. Structure and function of cytochromes // Annu. Rev. Biochem. 1977. Vol. 46. P. 299—330.
1294. Salioz M. Dicyclohexylcarbodiimide as a probe for proton translocating enzymes // Trends Biochem. Sci. 1984. Vol. 9. P. 309—312.
1295. Sallman A . L., Lubansky H. J., Talor 2., Arruda J. A. L. Plasma membrane proton ATPase from human kindey//Europ. J. Biochem. 1986. Vol. 157. P. 547—551.
1296. Saltzgaber-Miiller Kunapuli S. P., Douglas M. G. Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the Fx—ATPase subunit//J. Biol. Chem. 1983. Vol. 258. P. 11465—11470.
1297. Salviati G., Salvatori S., Betto R., MargrethA. Molecular and antigenic properties of cytochrome bb from slow-muscle sarcoplasmic reticulum // Biochem. J. 1981. Vol. 197. P. 515—518.
1298. Sandmann G., Malkin R. Light inhibition of respiration is due to a dual function of the cytochrome be— / complex and tne plastocyanin / cytochrome e553 pool in Aphanocapsa // Arch. Biochem. a. Biophys. 1984. Vol. 234. P. 105—111.
1299. Santore U. Greenwood A. D. The mitochondrial complex in Cryptop-hyceae//Arch. Microbiol. 1977. Vol. 112. P. 207—218.
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1301. Saraste M. Location of haem-binding sites in the mitochondrial cytochrome b // FEBS Lett. 1984. Vol. 166. P. 367—372.
1302. Saraste M., Deatherage M. A ., Naughton M. A ., Runswick M. J., Walker J. E. ATP—synthase and Fi—ATPase from bovine mitochondria //
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1304. Saraste M., RaitioM., Jalli Т., Peramaa A. A gene in Paracoccus for subunit III of cytochrome oxidase // FEBS Lett. 1986. Vol. 206. P. 154—156.
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