Immunological assays of the NADH dehydrogenase content of bovine heart mitochondria and submitochondrial particles
1980; Wiley; Volume: 110; Issue: 2 Linguagem: Inglês
10.1016/0014-5793(80)80092-5
ISSN1873-3468
AutoresStuart Smith, Ian Cottingham, C I Ragan,
Tópico(s)Hemoglobin structure and function
ResumoFEBS LettersVolume 110, Issue 2 p. 279-282 Full-length articleFree Access Immunological assays of the NADH dehydrogenase content of bovine heart mitochondria and submitochondrial particles Stuart Smith, Stuart Smith Department of Biochemistry, University of Southampton, Southampton, Hants S09 3TU, EnglandSearch for more papers by this authorIan R. Cottingham, Ian R. Cottingham Department of Biochemistry, University of Southampton, Southampton, Hants S09 3TU, EnglandSearch for more papers by this authorC.Ian Ragan, C.Ian Ragan Department of Biochemistry, University of Southampton, Southampton, Hants S09 3TU, EnglandSearch for more papers by this author Stuart Smith, Stuart Smith Department of Biochemistry, University of Southampton, Southampton, Hants S09 3TU, EnglandSearch for more papers by this authorIan R. Cottingham, Ian R. Cottingham Department of Biochemistry, University of Southampton, Southampton, Hants S09 3TU, EnglandSearch for more papers by this authorC.Ian Ragan, C.Ian Ragan Department of Biochemistry, University of Southampton, Southampton, Hants S09 3TU, EnglandSearch for more papers by this author First published: February 11, 1980 https://doi.org/10.1016/0014-5793(80)80092-5Citations: 16AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 T. Cremona, E.B. Kearney, J. Biol. Chem., 239, (1964), 2828– 2834. 2 R.F. Baugh, T.E. King, Biochem. Biophys. Res. Commun., 49, (1972), 1165– 1173. 3 C.I. Ragan, Biochem. J., 172, (1978), 539– 547. 4 E. Racker, Proc. Natl. Acad. Sci. USA, 48, (1962), 1657– 1663. 5 Y. Hatefi, J.S Rieske, Methods Enzymol., 10, (1967), 235– 239. 6 C. Heron, S. Smith, C.I. Ragan, Biochem. J., 181, (1979), 435– 443. 7 S. Smith, C.I. Ragan, Biochem. J., (1980), in press 8 E.J. Faeder, L.M. Siegel, Anal. Biochem., 53, (1973), 332– 336. 9 V. Massey, B.E.P. Swoboda, Biochem. Z., 338, (1963), 474– 484. 10 B.D. Nelson, I. Mendel-Hartvig, Eur. J. Biochem., 80, (1977), 267– 274. 11 T.E. King, R.L. Howard, Methods Enzymol., 10, (1967), 275– 294. 12 O.H. Lowry, N.J. Rosebrough, A.L. Farr, R.J. Randall, J. Biol. Chem., 193, (1951), 265– 275. 13 S. Smith, C.I. Ragan, Biochem. Soc. Trans., 6, (1978), 1349– 1352. 14 C.J. Lusty, J.M. Machinist, T.P. Singer, J. Biol. Chem., 240, (1965), 1804– 1810. 15 P-K. Huang, R.L. Pharo, Biochim. Biophys. Acta, 245, (1971), 240– 244. 16 M. Gutman, T.P. Singer, J.E. Casida, J. Biol. Chem., 245, (1970), 1992– 1997. 17 D.J. Horgan, H. Ohno, T.P. Singer, J. Biol. Chem., 243, (1968), 5967– 5976. 18 S.P.J. Albracht, F.J. Leeuwerik, B. Van Swol, FEBS Lett., 104, (1979), 197– 200. Citing Literature Volume110, Issue2February 11, 1980Pages 279-282 ReferencesRelatedInformation
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