1‐Anilino‐8‐naphthalene sulfonate binding as a probe for substrate mediated change in conformation of transaldolase
1970; Wiley; Volume: 7; Issue: 3 Linguagem: Inglês
10.1016/0014-5793(70)80169-7
ISSN1873-3468
Autores Tópico(s)Amino Acid Enzymes and Metabolism
ResumoFEBS LettersVolume 7, Issue 3 p. 235-238 Full-length articleFree Access 1-Anilino-8-naphthalene sulfonate binding as a probe for substrate mediated change in conformation of transaldolase K. Brand, K. Brand Max-Planck-Institut für Ernährungsphysiologie, Dortmund, GermanySearch for more papers by this author K. Brand, K. Brand Max-Planck-Institut für Ernährungsphysiologie, Dortmund, GermanySearch for more papers by this author First published: April 16, 1970 https://doi.org/10.1016/0014-5793(70)80169-7Citations: 17AboutPDF 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 Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 B.L. Horecker, P.Z. Smyrniotis, H.H. Hiatt, P.A. Marks, J. Biol. Chem., 212, (1955), 827– 10.1016/S0021-9258(18)71021-1 CASPubMedWeb of Science®Google Scholar 2 R. Venkataraman, E. Racker, J. Biol. Chem., 236, (1961), 1883– 10.1016/S0021-9258(18)64099-2 CASPubMedWeb of Science®Google Scholar 3 O. Tsolas, B.L. Horecker, Arch. Biochem. Biophys., 136, (1970), 303– 10.1016/0003-9861(70)90354-1 CASPubMedWeb of Science®Google Scholar 4 B.L. Horecker, S. Pontremoli, C. Ricci, T. Cheng, Proc. Natl. Acad. Sci. U.S., 47, (1961), 1940– 10.1073/pnas.47.12.1949 Web of Science®Google Scholar 5 B.L. Horecker, T. Cheng, S. Pontremoli, J. Biol. Chem., 238, (1963), 3428– 10.1016/S0021-9258(18)48684-X CASPubMedWeb of Science®Google Scholar 6 K. Brand, O. Tsolas, B.L. Horecker, Arch. Biochem. Biophys., 130, (1969), 521– 10.1016/0003-9861(69)90065-4 CASPubMedWeb of Science®Google Scholar 7 G. Weber, L.B. Young, J. Biol. Chem., 239, (1963), 1415– 10.1016/S0021-9258(18)91331-1 PubMedWeb of Science®Google Scholar 8 L. Stryer, J. Mol. Biol., 13, (1965), 482– 10.1016/S0022-2836(65)80111-5 CASPubMedGoogle Scholar 9 W.O. McChure, G.M. Edelman, Biochemistry, 5, (1966), 1908– 10.1021/bi00870a018 PubMedWeb of Science®Google Scholar 10 W. Thompson, K.L. Yielding, Arch. Biochem. Biophys., 126, (1968), 399– 10.1016/0003-9861(68)90424-4 CASPubMedWeb of Science®Google Scholar 11 S. Pontremoli, B.D. Prandini, A. Bonsignore, B.L. Horecker, Proc. Natl. Acad. Sci. U.S., 47, (1961), 1942– 10.1073/pnas.47.12.1942 CASPubMedWeb of Science®Google Scholar 12 J.N. Baxter, E.R. Perkin, F.J. Simpson, Can. J. Biochem. Physiol., 37, (1959), 199– 10.1139/o59-022 CASPubMedWeb of Science®Google Scholar 13 O. Tchola, B.L. Horecker, W.A. Wood Methods in Enzymology 9, (1966), Academic Press New York 499– Google Scholar 14 T. Bücher, Biochim. Biophys. Acta, 1, (1947), 292– 10.1016/0006-3002(47)90143-1 CASWeb of Science®Google Scholar 15 I.M. Klotz, F.M. Walker, R.B. Bivan, J. Am. Chem. Soc., 68, (1946), 1486– 10.1021/ja01212a030 CASPubMedWeb of Science®Google Scholar 16 S. Pontremoli, A. Bonsignore, E. Grazi, B.L. Horecker, J. Biol. Chem., 235, (1960), 1881– 10.1016/S0021-9258(18)69329-9 CASPubMedWeb of Science®Google Scholar 17 K. Brand, B.L. Horecker, Z. Anal. Chem., 243, (1968), 640– 10.1007/BF00530758 CASGoogle Scholar 18 B.L. Horecker, Pentose Metabolism in Bacteria (1962), Wiley New York 81– Google Scholar Citing Literature Volume7, Issue3April 16, 1970Pages 235-238 ReferencesRelatedInformation
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