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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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271. Blumwald E., Fortin M. G., Rea Pa, VermaD. P. S., Poole R. J. Presence of host-plasma membrane type H+—ATPase in the membrane en-
466
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velope enclosing the bacteroids in soybean root nodules // Plant Physiol.
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272. Blumwald E., Poole R. Na+/H+ antiport in isolated tonoplast vesicles from storage tissue of Beta vulgaris // Ibid. P. 163—167.
273. BodieA. F., Gray С. T. Phosphorylation coupled to oxidation in bacterial extracts// J. Biol. Chem. 1956. Vol. 219. P. 853—862.
274. BoekemaE.J., Berden J. A., Van Heel M. G. Structure of mitochondrial Fx—ATPase studied by electron microscopy and image processing // Biochim. et biophys. acta. 1986. Vol. 851. P. 353—360.
275. Bogomolni R. A., Spudich J. L. Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium//Proc. Nat. Acad. Sci. US. 1982. Vol. 79. P. 6250—6254.
276. Bogomolni R. A ., Taylor M.E., Stoeckenius W. Reconstitution of purified halorhodopsin//Ibid. 1984. Vol. 81. P. 5408—5411.
277. Bokranz М., Morschel E., Kroger A. Structural and ATP-hydrolyzing properties of the ATP synthase isolated from Wolinella succinogenes// Biochim. et biophys. acta. 1985. Vol. 810. P. 84—93.
278. Bombelka E., Richter F.-W., StrohA., KadenbachB. Analysis of the Cu, Fe, and Zn contents in cytochrome с oxidase // Biochem. a Biophys. Res. Commun. 1986. Vol. 140. P. 1007—1014.
279. Bonaventura C., Myers J. Fluorescence and oxygen evolution from Chlo-rella pyrenoidosa//Biochim. et . boiphys. acta. 1969. Vol. 189. P. 366—383.
280. Bonitz S. G., Coruzzi C., ThalenfeldB. E., Tzagoloff A., Macino G. Assembly of mitochondrial membrane system. Structure and nucleotide sequence of the gene coding for subunit I of yeast cytochrome oxidase // J. Biol. Chem. 1980. Vol. 255. P. 11927—11941.
281. Bonnerjea J. R., Evans М. C. W. Evidence that the lowpotential (—700 mV) electron acceptor (X) in photosystem I has two iron-sulphur centres // Biochim. et biophys. acta. 1984. Vol. 767. P. 153—159.
282. Borchart U., Machleidt W., Schagger H., Link T. A., JagowG. von. Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of beef heart ubiquinol: cytochrome с reductase // FEBS Lett. 1985. Vol.
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283. Borchart U., Machleidt W., Schagger H., Link T. A., Jagow G. von. Isolation and amino acid sequence of the 9.5 kDa protein of beef heart ubiquinol: cytochrome с reductase // Ibid. 1986. Vol. 200. P. 81—86.
284. BorgstrSm B., Sudduth H. C., Lehninger A . L. Phosphorylation coupled reduction of cytochrome с by (3-hydroxybutirate // J. Biol. Chem. 1955. Vol. 215. P. 571—577.
285. Borisov A. Yu,., Godik V. I. Excitation energy transfer in photosynthesis// Biochim. et biophys. acta. 1973. Vol. 301. P. 221—248.
286. Bouilland F., Ricquier О., Gulik-Krzywicki Т., Gary-Bobo С. M. The possible proton translocating activity of the mitochondrial uncoupling protein of brown adipose tissue // FEBS Lett. 1983. Vol. 164. P. 272—276.
287. Bouilland F., Ricquier D., Thibault J., Weissenbach J. Molecular approach to thermogenesis in brown adipose tissue: cDNA cloning of the mitochondrial uncoupling protein//Proc. Nat. Acad. Sci. US. 1985. Vol. 82. P. 445—448.
288. Bouilland F., Weissenbach J., Ricquier D. Complete cDNA-derived amino acid sequence of rat brown fat uncoupling protein// J. Biol. Chem. 1986. Vol. 261. P. 1487—1490.
289. Boutry М., Briquet М., GoffeauA. The subunit of a plant mitochondrial Fj—ATPase is translated in mitochondria // Ibid. 1983. Vol. 258. P. 8524—8526.
290. Bowman E. J. Comparison of the vacuolar membrane ATPase of Neuro-spora crassa with the mitochondrial and plasmic membrane ATPases // Ibid. 1983. Vol. 258. P. 15238—15244.
Список литературы
467
291. Bowman E.J., Bowman В. J. С. Identification and properties of an ATPase in vacuolar membranes of Neurospora crassa//J. Bacteriol.
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292. Boyer P. DCross R. L., Momsen W. A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions // Proc. Nat. Acad. Sci. US. 1973. Vol. 70. P. 2837—2839.
293. Bragg P. D. The ATPase complex of Escherichia coli // Canad. J. Biochem. a. Cell Biol. 1984. Vol. 62. P. 1190—1197.
294. Bragg P. D., HouC. Chemical crosslinking of a-subunit in the Fi adenosine triphosphatase of Escherichia coli // Arch. Biochem. a. Biophys.
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295. Brand M. D., Al-Shawi М. K., Brown G. C., Price В. D. Thermodynamic and steady-state-kinetic investigation of the effect of N,N'-dicyclo-hexylcarbodiimide on H+ translocation by the mitochondrial cytochrome Ъсг complex//Biochem. J. 1985. Vol. 225. P. 407—411.
296. Brandolin G., Doussiere J., Gulik A., Gulik-Krzywicki Т., Lauqu-in G. J. М., Vignais P. V. Kinetic, binding and ultrastructural properties of the beef heart adenine nucleotide carrier protein after incorporation into phospholipid vesicles // Biochim. et biophys. acta. 1980. Vol.
592. P. 592—614.
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