Plasma Nτ-methylhistidine concentration is a sensitive index of myofibrillar protein degradation during starvation in rats

Bioscience, Biotechnology and Biochemistry

Volumn 60, Issue 3, 1996, Pages 501-502

  Nagasawa, Takashi ^a   Yoshizawa, Fumiaki ^b   Nishizawa, Naoyuki ^a  

^a IWATE UNIVERSITY   (Japan)

^b Iwate Pref Morioka Junior College   (Japan)

Author keywords

3 methylhistidine; Myofibrillar protein; Protein degradation; Starvation

Indexed keywords

3 METHYLHISTIDINE; 3-METHYLHISTIDINE; HISTIDINE DERIVATIVE; MUSCLE PROTEIN;

ANIMAL; ARTICLE; BLOOD; BODY WEIGHT; HISTOLOGY; METABOLISM; MUSCLE; ORGAN SIZE; PHYSIOLOGY; RAT; SENSITIVITY AND SPECIFICITY; SPRAGUE DAWLEY RAT; STARVATION; URINE;

ANIMALS; BODY WEIGHT; METHYLHISTIDINES; MUSCLE PROTEINS; MUSCLES; ORGAN SIZE; RATS; RATS, SPRAGUE-DAWLEY; SENSITIVITY AND SPECIFICITY; STARVATION;

EID: 0030093797     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60.501     Document Type: Article

References (24)

1. R. Funabiki. in “Nutrition: Proteins and Amino Acids," ed. by A. Yoshida. H. Naito, T. Niivama, and T. SuJ.uki, Japan Scientific Societies Press, Tokyo and Springer Verlag, Berlin, 1990, pp. 35-48.
2. D. J. Millward, P. J. Garlick, W. P. T. James, D. O. Nnaryelugo, and J. S. Rtatt, Nature, 241, 204 (1973).
3. N. Nishizawa, M. Shimbo, T. Noguchi, S. Hareyama, and R. Funabiki. Agrie. Biol. Chem. 42, 2083-2089 (1978).
4. V. R. Young and H. N. Munro, Fed. Proc., 37. 2291-2300 (1978).
5. F. J. Ballard and F. M. Tomas, Clin. Sci., 65, 209-215 (1983).
6. D. R. Rao, B. Elyaskordi, S. R. Pulusani, and C. B. Chawan, Nutr. Rep. hu. 26, 355-364 (1982).
7. K. Bachmann, R. Galeazzi, A. Millet, and A. G. Burger. Metabolism, 33, 107-110 (1984).
8. T. Nagasawa, N. Hashiguehi, and R. Onodera, Biosci. Biotech. Biochem., 57. 517 (1993).
9. American Institute of Nutrition, J. Nutr., 107. 1340-1348 (1977).
10. V. E. Baracos, E. J. Wilson, and A. L. Goldberg, Am. J. Physiol., 246, Cl25- Cl30 (1984). '
11. T. Nagasawa, T. Sakai, and R. Onodera, J. Chromatogr., 566, 223-227(1991).
12. M. Kadowaki, N. Harada, S. Takahashi, T. Noguchi, and FI. Naito, J. Nutr. 119, 471-477 (1989).
13. N. Nishizawa, M. Shimbo, S. Hareyama, and R. Funabiki, Br. J. Nutr., 37. 345-353 (1977). "
14. V. R. Young, S. D. Alexis, B. S. Baliga, H. N. Munro, and W. Muecke. J. Biol. Chem., 247. 3592-3600 (1972).
15. D. J. Millward, P. C. Bates, G. K. Grimble, J. G. Brown, M. Nathan, and M. J. Rennie, Bioehem. J., 190. 225-228 (1980).
16. P. W. Emery, L. Cotellessa, M. Holness, C. Egan, and M. J. Rennie. Biosei. Rep., 6. 143-153 (1986).
17. N. Nishizawa, T. Noguchi, S. Hareyama, and R. Funabiki, Br. J. Nutr., 38. 149-151 (1977).
18. T. Nagasawa and R. Funabiki. J. Biochem. (Tokyo), 89, 1155-1161 (1981).
19. C. I. Harris, Biochem. J., 194. 1011-1014 (1981).
20. M. Kadowaki, T. Nagasawa, T. Hirata, T. Noguchi, and H. Naito, J. Nutr. Sei. Vitaminol. 31, 431-440 (1985).
21. T. Seene, J. Steroid Biochem. Molee. Biol., 50, 1-4 (1994).
22. R. Belkhou, D. Bechet, Y. Cherel, M. Galluser, M. Ferrara, and Y. Le Maho. Biochem. Biophys. Acta, 1199, 195-201 (1994).
23. M. A. Ilian and N. E. Forsberg, Biochem. J., 287, 163-171 (1992).
24. S. S. Wing and A. L. Goldberg. Am. J. Physiol. 264. E668 -E676 (1993).