FEBS LettersVolume 51, Issue 1-2 p. 112-115 Full-length articleFree Access Restoration of reconstitutive capacity of succinate dehydrogenase by rhodanese S. Pagani, S. Pagani Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this authorC. Cannella, C. Cannella Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this authorP. Cerletti, P. Cerletti Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this authorL. Pecci, L. Pecci Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this author S. Pagani, S. Pagani Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this authorC. Cannella, C. Cannella Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this authorP. Cerletti, P. Cerletti Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this authorL. Pecci, L. Pecci Department of General Biochemistry, University of Milan and Department of Biological Chemistry, University of Rome, Rome, ItalySearch for more papers by this author First published: March 01, 1975 https://doi.org/10.1016/0014-5793(75)80865-9Citations: 11AboutPDF 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 S. Pagani, F. Bonomi, P. Cerletti, FEBS Lett., 39, (1974), 139– 143. 2 D.V. Dervartanian, C. Veeger, Johnson W.H. Orme, H. Beinert, Biochim. Biophys. Acta, 191, (1969), 22– 37. 3 M.L. Baginsky, Y. Hatefi, J. Biol. Chem., 244, (1969), 5313– 5319. 4 W.G. Hanstein, K.A. Davis, M.A. Ghalambor, Y. Hatefi, Biochemistry, 10, (1971), 2517– 2524. 5 T.E. King, J. Biol. Chem., 238, (1963), 4037– 4051. 6 T. Kimura, J. Hauber, Biochem. Biophys. Res. Commun., 13, (1963), 169– 174. 7 T.E. King, Biochem. Biophys. Res. Commun., 16, (1961), 511– 515. 8 P. Bernath, T.P. Singer, S.P. Colowick N.O. Kaplan Methods in Enzymology 5, (1962), Academic Press New York 597– 9 Agrò A. Pinazzi, C. Cannella, M.T. Graziani, D. Cavallini, FEBS Lett., 16, (1971), 172– 174. 10 P. Cerletti, G. Zanetti, G. Testolin, C. Rossi, F. Rossi, G. Osenga, H. Kamin Flavins and flavoproteins (1971), University Park Press Baltimore 629– 11 T.E. King, R.W. Estabrook M.E. Pullman Methods in Enzymology 10, (1967), Academic Press New York 202– 12 C. Cannella, L. Pecci, G. Federici, Italian J. Biochem., 21, (1972), 1– 7. 13 P. Cerletti, M.A. Giovenco, M.G. Giordano, S. Giovenco, R. Strom, Biochim. Biophys. Acta, 146, (1967), 380– 396. 14 B.H. Sörbo, Acta Chem. Scand., 7, (1953), 1129– 1136. 15 T.E. King, R.O. Morris, R.W. Estabrook M.E. Pullman Methods in Enzymology X, (1967), Academic Press New York 634– 16 R.F. Itzhaki, O.M. Gill, Anal. Biochem., 9, (1964), 401– 410. 17 P. Cerletti, M.G. Giordano, D. McCormick Wright Methods in Enzymology 18B, (1971), Academic Press New York 285– 18 D. Petering, J.A. Fee, G. Palmer, J. Biol. Chem., 246, (1971), 634– 653. 19 J. Westley, Advances Enzymol., 39, (1973), 327– 368. Citing Literature Volume51, Issue1-2March 01, 1975Pages 112-115 ReferencesRelatedInformation