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The control of haemoglobin synthesis: factors controlling theoutput of α and β chains

Published online by Cambridge University Press:  24 January 2017

R. T. Hunt ,
A. R. Hunter  and
A. J. Munro
R. T. Hunt
Affiliation:
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge
A. R. Hunter
Affiliation:
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge
A. J. Munro
Affiliation:
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge
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Analysis of the effects of amino acid starvation in reticulocytes iscomparatively simple compared with similar analysis in other tissues ofwhole organisms. This is mainly because of the absence of RNA synthesis inreticulocytes, but also because the bulk of the protein being synthesized ishaemoglobin, a protein whose structure is completely known. The absence ofRNA synthesis eliminates complications that would otherwise arise throughRNA-mediated control mechanisms which in turn might mask the effects ofamino acid starvation on the protein synthetic machinery in the cells(Munro, 1969). Consequently reticulocytes have been used to study the effectof amino acid starvation on the actual process of protein synthesis andassembly.

Information

Type
Symposium Proceedings
Information
Proceedings of the Nutrition Society , Volume 28 , Issue 2 , September 1969 , pp. 248 - 254
Copyright
Copyright © Proceedings of the Nutrition Society 1969

References

Baglioni, C. & Campana, T. (1967). Eur. J. Biochem. 2, 480.10.1111/j.1432-1033.1967.tb00162.xGoogle Scholar
Baglioni, C., Campana, T. & Colombo, B. (1966). Archs Biochem. Biophys. 117, 515.10.1016/0003-9861(66)90092-0Google Scholar
Bruns, G. P. & London, I. M. (1965). Biochem. biophys. Res. Commun. 18, 236.10.1016/0006-291X(65)90746-1Google Scholar
Colombo, B. & Baglioni, C. (1966). J. molec. Biol. 16, 51.10.1016/S0022-2836(66)80262-0Google Scholar
Hori, M., Fisher, J. M. & Rabinovitz, M. (1967). Science, N. Y. 155, 83.10.1126/science.155.3758.83Google Scholar
Hori, M. & Rabinovitz, M. (1968). Proc. natn. Acad. Sci. U.S.A. 59, 1349.10.1073/pnas.59.4.1349Google Scholar
Huehns, E. R., Dance, N., Shooter, E. M. & Beaven, G. H. (1962). J. molec. Biol. 5, 511.10.1016/S0022-2836(62)80124-7Google Scholar
Hunt, R. T., Hunter, A. R. & Munro, A. (1968α). J. molec. Biol. 36, 31.10.1016/0022-2836(68)90217-9Google Scholar
Hunt, R. T., Hunter, A. R. & Munro, A. J. (1968ο). Nature, Lond. 220, 481.10.1038/220481a0Google Scholar
Hunt, R. T., Hunter, A. R. & Munro, A. J. (1969). J. molec. Biol. 43, 123.10.1016/0022-2836(69)90083-7Google Scholar
Itano, H. A. (1966). J. cell. comp. Physiol. 67, 65.10.1002/jcp.1040670408Google Scholar
Kazazian, H. H. Jr & Freedman, M. L. (1968). J. biol. Chem. 243, 6446.Google Scholar
Lingrel, J. B. & Borsook, H. (1963). Biochemistry, Easton 2, 309.10.1021/bi00902a022Google Scholar
Munro, H. N. (1969). Proc. Nutr. Soc. 28, 214.10.1017/S0029665100100114Google Scholar
Schweiger, H. G., Rapoport, S. & Scholzel, F. (1956). Z. Physiol. Chem. 306, 33.Google Scholar
Shaeffer, J. R., Trostle, P. K. & Evans, R. F. (1967). Science, N. Y. 158, 488.10.1126/science.158.3800.488Google Scholar
Tavili, A. S., Grayzel, A. L, London, I. M., Williams, M. K. & Vanderhoff, G. A. (1968). J. biol. Chem. 243, 4987.Google Scholar
Waxman, H. S. & Rabinovitz, M. (1966). Biochim. biophys. Acta 129, 369.10.1016/0005-2787(66)90379-0Google Scholar
Winslow, R. M. & Ingram, V. M. (1966). J. biol. Chem. 241, 1144.Google Scholar