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Association of iron‐protoporphyrin‐IX (hemin) with myosins

1990; Wiley; Volume: 266; Issue: 1-2 Linguagem: Inglês

10.1016/0014-5793(90)81493-8

1873-3468

V. Bhoite-Solomon, Gania Kessler‐Icekson, Nurith Shaklai,

Hemoglobin structure and function

FEBS LettersVolume 266, Issue 1-2 p. 9-12 Full-length articleFree Access Association of iron-protoporphyrin-IX (hemin) with myosins V. Bhoite-Solomon, Corresponding Author V. Bhoite-SolomonSearch for more papers by this authorG. Kessler-Icekson, G. Kessler-IceksonSearch for more papers by this authorN. Shaklai, N. ShaklaiSearch for more papers by this author V. Bhoite-Solomon, Corresponding Author V. Bhoite-SolomonSearch for more papers by this authorG. Kessler-Icekson, G. Kessler-IceksonSearch for more papers by this authorN. Shaklai, N. ShaklaiSearch for more papers by this author First published: June 18, 1990 https://doi.org/10.1016/0014-5793(90)81493-8Citations: 10AboutPDF 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. Yoda, L.G. Israels, Can. J. Biochem., 50, (1972), 633– 639. 10.1139/o72-087 CASPubMedWeb of Science®Google Scholar 2 E. Tipping, B. Ketterer, Biochem. J., 195, (1981), 441– 447. 10.1042/bj1950441 CASPubMedWeb of Science®Google Scholar 3 I. Kirschner-Zilber, H. Laufer, N. Shaklai, J. Cell. Biochem., 41, (1989), 113– 123. 10.1002/jcb.240410302 CASPubMedWeb of Science®Google Scholar 4 W.T. Morgan, H.H. Liem, R.G. Sutor, U. Muller-Eberhard, Biochim. Biophys. Acta, 444, (1976), 435– 445. 10.1016/0304-4165(76)90387-1 CASPubMedWeb of Science®Google Scholar 5 U. Muller-Eberhard, Methods Enzymol., 163, (1988), 536– 565. 10.1016/0076-6879(88)63049-7 CASPubMedWeb of Science®Google Scholar 6 M. Vache, C. Nicot, M. Pellum, J. Luchins, S. Beychok, M. Waks, Arch. Biochem. Biophys., 231, (1984), 95– 101. 10.1016/0003-9861(84)90366-7 PubMedWeb of Science®Google Scholar 7 G.H. Beaven, W.B. Gratzer, Acta Haematol., 60, (1978), 321– 328. 10.1159/000207731 CASPubMedWeb of Science®Google Scholar 8 I. Solar, N. Shaklai, Biochim. Biophys. Acta, 983, (1989), 199– 204. 10.1016/0005-2736(89)90234-4 CASPubMedWeb of Science®Google Scholar 9 N. Avissar, M. Shaklai, N. Shaklai, Biochim. Biophys. Acta, 786, (1984), 179– 187. 10.1016/0167-4838(84)90087-6 CASPubMedWeb of Science®Google Scholar 10 P. Cummins, Biochem. J., 205, (1982), 195– 204. 10.1042/bj2050195 CASPubMedWeb of Science®Google Scholar 11 H. Shlesinger, Y. Ovil, M.J. Levy, G. Kessler-Icekson, Biochem. Int., 11, (1985), 747– 753. CASPubMedWeb of Science®Google Scholar 12 O.H. Lowry, N.J. Rosenbrough, A.L. Farr, R.J. Randall, J. Biol. Chem., 193, (1951), 265– 275. 10.1016/S0021-9258(19)52451-6 CASPubMedWeb of Science®Google Scholar 13 J.F.Y. Hoh, P.A. MacGrath, P.T. Hale, J. Mol. Cell. Cardiol., 10, (1977), 1053– 1076. 10.1016/0022-2828(78)90401-7 CASPubMedWeb of Science®Google Scholar 14 E. Antononi, M. Brunori, Hemoglobin and Myoglobin in Their Reactions with Ligands, (1971), Chapter 3 Google Scholar Citing Literature Volume266, Issue1-2June 18, 1990Pages 9-12 ReferencesRelatedInformation