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Ornithine decarboxylase in phytohaemagglutinin stimulated lymphocytes: Control of degradation rate by amino acids

1972; Wiley; Volume: 21; Issue: 2 Linguagem: Inglês

10.1016/0014-5793(72)80118-2

1873-3468

John E. Kay, Valerie J. Lindsay, Anne Cooke,

GABA and Rice Research

FEBS LettersVolume 21, Issue 2 p. 123-126 Full-length articleFree Access Ornithine decarboxylase in phytohaemagglutinin stimulated lymphocytes: Control of degradation rate by amino acids John E. Kay, Corresponding Author John E. Kay Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, Sussex, EnglandTo whom to address correspondence.Search for more papers by this authorValerie J. Lindsay, Valerie J. Lindsay Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, Sussex, EnglandSearch for more papers by this authorAnne Cooke, Anne Cooke Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, Sussex, EnglandSearch for more papers by this author John E. Kay, Corresponding Author John E. Kay Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, Sussex, EnglandTo whom to address correspondence.Search for more papers by this authorValerie J. Lindsay, Valerie J. Lindsay Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, Sussex, EnglandSearch for more papers by this authorAnne Cooke, Anne Cooke Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, Sussex, EnglandSearch for more papers by this author First published: March 15, 1972 https://doi.org/10.1016/0014-5793(72)80118-2Citations: 21AboutPDF 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 D.H. Russell, S.H. Snyder, Proc. Natl. Acad. Sci. U.S., 60, (1968), 1420– 10.1073/pnas.60.4.1420 CASPubMedWeb of Science®Google Scholar 2 J. Jänne, A. Raina, Biochim. Biophys. Acta, 174, (1969), 769– 10.1016/0005-2787(69)90310-4 CASPubMedWeb of Science®Google Scholar 3 M. Stastny, S. Cohen, Biochim. Biophys. Acta, 204, (1970), 578– 10.1016/0005-2787(70)90177-2 CASPubMedWeb of Science®Google Scholar 4 J.E. Kay, A. Cooke, FEBS Letters, 16, (1971), 9– 10.1016/0014-5793(71)80671-3 CASPubMedWeb of Science®Google Scholar 5 B.L.M. Hogan, Biochem. Biophys. Res. Commun., 45, (1971), 301– 10.1016/0006-291X(71)90818-7 CASPubMedWeb of Science®Google Scholar 6 D.H. Russell, S.H. Snyder, Mol. Pharmacol., 5, (1969), 253– CASPubMedWeb of Science®Google Scholar 7 D.H. Russell, V.J. Medina, S.H. Snyder, J. Biol. Chem., 245, (1970), 6732– 10.1016/S0021-9258(18)62595-5 CASPubMedWeb of Science®Google Scholar 8 D.H. Russell, Proc. Natl. Acad. Sci. U.S., 68, (1971), 523– 10.1073/pnas.68.3.523 CASPubMedWeb of Science®Google Scholar 9 H.L. Cooper, J. Biol. Chem., 243, (1968), 34– 10.1016/S0021-9258(18)99322-1 CASPubMedWeb of Science®Google Scholar 10 J.E. Kay, A. Korner, Biochem. J., 100, (1966), 815– 10.1042/bj1000815 CASPubMedWeb of Science®Google Scholar 11 A.E. Pegg, H.G. Williams-Ashman, Biochem. J., 108, (1968), 533– 10.1042/bj1080533 CASPubMedWeb of Science®Google Scholar 12 S.D. Handmaker, J.W. Graef, Biochim. Biophys. Acta, 199, (1970), 95– 10.1016/0005-2787(70)90698-2 CASPubMedWeb of Science®Google Scholar 13 E.A. Zylber, S. Penman, Biochim. Biophys. Acta, 204, (1970), 221– 10.1016/0005-2787(70)90505-8 CASPubMedWeb of Science®Google Scholar 14 J.E. Kay, T. Ahern, M. Atkins, Biochim. Biophys. Acta, 247, (1971), 322– 10.1016/0005-2787(71)90680-0 CASPubMedWeb of Science®Google Scholar 15 J.E. Kay, M.W. Elves The Biological Effects of PHA (1966), R. Jones and A. Hunt Orthopaedic Hospital Oswestry, England 37– Google Scholar 16 J.E. Kay, S.D. Handmaker, Exp. Cell Res., 63, (1970), 411– 10.1016/0014-4827(70)90230-2 CASPubMedGoogle Scholar 17 A. Cooke, J.E. Kay, H.L. Cooper, Biochem. J., 125, (1971), 74p– 10.1042/bj1250074Pa CASPubMedWeb of Science®Google Scholar 18 B.L.M. Hogan, A. Korner, Biochim. Biophys. Acta, 169, (1968), 129– 10.1016/0005-2787(68)90014-2 CASPubMedWeb of Science®Google Scholar 19 R. Shields and A. Korner, Biochim. Biophys. Acta, 204, 521. Google Scholar 20 M.H. Vaughan, P.J. Pawlowski, J. Forchhammer, Proc. Natl. Acad. Sci. U.S., 68, (1971), 2057– 10.1073/pnas.68.9.2057 CASPubMedWeb of Science®Google Scholar 21 D.H. Russell, S.H. Snyder, V.J. Medina, Endocrinology, 98, (1970), 1414– 10.1210/endo-86-6-1414 Web of Science®Google Scholar 22 N. Fausto, Biochim. Biophys. Acta, 238, (1971), 116– 10.1016/0005-2787(71)90015-3 CASPubMedWeb of Science®Google Scholar 23 A. Hershko, G.M. Tomkins, J. Biol. Chem., 246, (1971), 710– 10.1016/S0021-9258(18)62470-6 CASPubMedWeb of Science®Google Scholar Citing Literature Volume21, Issue2March 15, 1972Pages 123-126 ReferencesRelatedInformation