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Regulation of the degradation of 125 I‐labeled glutamine synthetase introduced into cultured hepatoma cells by erythrocyte ghost—mediated injection

1981; Wiley; Volume: 128; Issue: 1 Linguagem: Inglês

10.1016/0014-5793(81)81080-0

1873-3468

Aliza Freikopf-Cassel, Richard G. Kulka,

Toxin Mechanisms and Immunotoxins

FEBS LettersVolume 128, Issue 1 p. 63-66 Full-length articleFree Access Regulation of the degradation of 125I-labeled glutamine synthetase introduced into cultured hepatoma cells by erythrocyte ghost—mediated injection Aliza Freikopf-Cassel, Aliza Freikopf-Cassel Department of Biological Chemistry, The Hebrew University of Jerusalem, Institute of Life Sciences, 91904 Jerusalem, IsraelSearch for more papers by this authorRichard G. Kulka, Richard G. Kulka Department of Biological Chemistry, The Hebrew University of Jerusalem, Institute of Life Sciences, 91904 Jerusalem, IsraelSearch for more papers by this author Aliza Freikopf-Cassel, Aliza Freikopf-Cassel Department of Biological Chemistry, The Hebrew University of Jerusalem, Institute of Life Sciences, 91904 Jerusalem, IsraelSearch for more papers by this authorRichard G. Kulka, Richard G. Kulka Department of Biological Chemistry, The Hebrew University of Jerusalem, Institute of Life Sciences, 91904 Jerusalem, IsraelSearch for more papers by this author First published: June 01, 1981 https://doi.org/10.1016/0014-5793(81)81080-0Citations: 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 R. De Mars, Biochim. Biophys. Acta, 27, (1958), 435– 436. 2 J. Paul, P.F. Fortrell, Biochim. Biophys. Acta, 67, (1963), 334– 336. 3 R.G. Kulka, G.M. Tomkins, R.B. Crook, J. Cell Biol., 54, (1972), 175– 179. 4 D.C. Tiemeier, G. Milman, J. Biol. Chem., 247, (1972), 5722– 5727. 5 G. Arad, A. Freikopf, R.G. Kulka, Cell, 8, (1976), 95– 101. 6 R.G. Kulka, H. Cohen, J. Biol. Chem., 248, (1973), 6738– 6743. 7 A. Friekopf, R.G. Kulka, Biochem. Biophys. Res. Commun., 72, (1976), 1195– 1200. 8 A. Freikopf, R.G. Kulka, Eur. J. Biochem., 56, (1975), 484– 492. 9 M. Wasserman, N. Zakai, A. Loyter, R.G. Kulka, Cell, 7, (1976), 551– 556. 10 S.S. Tate, F.Y. Leu, A. Meister, J. Biol. Chem., 247, (1972), 5312– 5321. 11 V.S. Fang, A.W. Cho, H.Y. Meltzer, Biochem. Biophys. Res. Commun., 65, (1975), 413– 419. 12 H.S. Penefsky, J. Biol. Chem., 252, (1977), 2891– 2899. 13 U.K. Laemmli, Nature, 227, (1970), 680– 685. 14 H. Umezawa, Enzyme Inhibitors of Microbiol Origin (1972), University of Tokyo Press 15 G. Arad, R.G. Kulka, Biochim. Biophys. Acta, 544, (1978), 153– 162. 16 R.T. Dean, Nature, 257, (1975), 414– 416. 17 M. Yamaizumi, T. Uchida, E. Mekada, Y. Okada, Cell, 18, (1979), 1009– 1014. 18 M. Zavortnik, T. Thatcher, M. Rechsteiner, J. Cell. Physiol., 100, (1979), 175– 186. 19 M. Wasserman, R.G. Kulka, A. Loyter, FEBS Lett., 83, (1977), 48– 52. 20 N.T. Neff, G.N. De Martino, A.L. Goldberg, J. Cell. Physiol., 101, (1979), 439– 458. 21 M.F. Hopgood, M.G. Clark, F.J. Ballard, Biochem. J., 164, (1977), 399– 407. Citing Literature Volume128, Issue1June 01, 1981Pages 63-66 ReferencesRelatedInformation