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1994 | 41 | 4 |

Tytuł artykułu

Differences in nonezymatic glycation of histones

Warianty tytułu

Języki publikacji

EN

Abstrakty

Time course of glucose binding by histone HI and total histones was followed in isolated histone preparations and in thymus nuclei. In both cases the uptake of glucose by HI was surprisingly high in contrast to a much lower uptake of glucose by total histones. DNA is not implicated in glycation of histones in nuclei.

Słowa kluczowe

EN

Wydawca

-

Rocznik

Tom

41

Numer

4

Opis fizyczny

p.429-432,fig.

Twórcy

autor
  • University Medical School, Pecs, Hungary
autor
autor

Bibliografia

  • 1. Csordas, A. (1990) On the biological role of histone acetylation. Biochcm. J. 265,23-38.
  • 2. Perry, C.A. & Annunziato, A.T. (1991) Histone acetylation reduces HI-mediated nucleosome interactions during chromatin assembly. Exp. Cell Res. 196,337-345.
  • 3. Pfeffer, U. & Vidali, G. (1991) Histone acetylation: recent approaches to a basic mechanism of genome organisation. Int. J. Biochent. 23,277-285.
  • 4. Turner, B.M. (1991) Histone acetylation and control of gene expression. /. Cell Sci. 99,13-20.
  • 5. De Bellis, D. & Horowitz, M.I. (1987) In vitro studies of histone glycation. Biochim. Biophys. Acta 926,365-368.
  • 6. Day, J.F. Thornburg, R.W.,Thorpe, S.R. & Baynes, J.W. (1979) Nonenzymatic glucosyla- tion of rat albumin. /. Biol. Chem. 254,9394-9400.
  • 7. Garlick, R.L. & Mazer, J.S. (1983) The principal site of nonenzymatic glycosylation of human serum albumin in vivo. J. Biol. Chem. 258, 6142-6246.
  • 8. Tberg, N. & Fluckinger, R. (1986) Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites. J. Biol. Chcin. 261, 13542-13545.
  • 9. Jobst, K., Lakatos, A. & HorvSth, A. (1991) Glycohistones in diabetic human liver. Clin. Chim. Acta 200,231-232.
  • 10. Allfrey, V.G., Littau, V.C. & Mirsky, D. (1964) Methods for the purification of thymus nuclei and their application to studies of nuclear protein synthesis. J. Cell Biol. 21,213-231.
  • 11. Bustin, M., Lehn, D.A. & Landsman, D. (1990) Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049,231-243.
  • 12. Johns, E.W. (1971) The preparation and characterization of histones; in Histones and Nucleohistones (Phillips, D.M.P., ed.) pp. 2-84, Plenum Press, London and New York.
  • 13. Csordas, A., Pedrini, M. & Grunicke, H. (1990) Suitability of staining techniques for the detection and quantitation of nonhistone high mobility group proteins. Electrophoresis 11, 118-123.
  • 14. Johnson, R.N., Metcalf, P.A. & Baker, J.R. (1982) Fructosamine: a new approach to the estimation of scrum glycosylprotein. An index of diabetic control. Clin. Chim. Acta 127,87-95.
  • 15. Bernstein, R.E. (1987) Nonenzymatically glycosylated proteins; in Advances in Clinical Chemistry (Spiegel, H.E., ed.) vol. 26, pp. 1-78, Academic Press Inc.
  • 16. Allen, J., I lartmann, P.G., Crane-Robinson, C. & Aviles, F.X. (1980) The structure of histone H 1 and its location in chromatin. Nature (London) 288,675-679.
  • 17. Allan, J., Harbome, N., Rau, D.C. & Gould, H. (1982) Participation of core histone "tails" of the chromatin solenoid. J. CHI Biol. 93,285-297.
  • 18. Lederer, B., Jobst, K. & Sandritter, W. (1966) Die Feulgen-Reaktion bei der Langzcithydrolyse: Der Einfluss von Histonprotein. Acta Histochem. 24,379-381 .
  • 19. Lakatos, A. & Jobst, K. (1989) Histone glycosylation. Acta Biochim. Biophys. Hung. 24, 355-359.
  • 20. Lee, A.T., & Cerami, A. (1987) The formation of reactive intermediates of glucose-6-phosphate and lysine capable of rapidly reacting with DNA. Mutation Res. 79,151-158.
  • 21. Wu, R.S., Panusz, H.T., Hatch, Ch.L. & Bonner, W.M. (1986) Histonesand theirmodifications; in Critical Reviews in Biochemistry 20,201-263.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-41922988-5f45-4807-9b02-e7131d6d6533
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