Effects of NAD or NADP on the stability of liver and pectoral muscle enzymes in 3-acetylpyridine treated quail by heat and trypsin

International Journal of Biochemistry and Cell Biology

Volumn 30, Issue 11, 1998, Pages 1223-1234

  Park, In Kook ^a   Kim, Jae Young ^a  

^a Dongguk University   (South Korea)

Author keywords

3 Acetylpyridine; Enzyme stability; Heat and trypsin treatment; Japanese quail; Niacin analogue

Indexed keywords

3 ACETYLPYRIDINE; ACETYLCHOLINESTERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTATE DEHYDROGENASE; LIVER ENZYME; MALATE DEHYDROGENASE (DECARBOXYLATING); MUSCLE ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHOGLUCONATE DEHYDROGENASE; TRYPSIN;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME INACTIVATION; FEMALE; HEAT; NONHUMAN; PECTORAL MUSCLE; QUAIL;

PHASIANIDAE;

EID: 0032212882     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(98)00088-0     Document Type: Article

References (32)

1. [1] H. Herken, Functional disorders of the brain induced by synthesis of nucleotides containing 3-acetylpyridine, Z. Kiln. Chem. 6 (1968) 357-367.
2. [2] M. Weller, A.M. Marini, S.M. Paul, Niacinamide blocks 3-acetylpyridine toxicity of cerebellar granule cells in vitro, Brain Res. 594 (1992) 160-164.
3. [3] W.A. Anderson, B.A. Flumerfelt, Sensitivity of rat inferior olivary neurons to 3-acetylpyridine, Brain Res. 12 (1984) 285-291.
4. [4] I.K. Park, S. Shin, R.R. Marquardt, Effects of niacin deficiency on the relative turnover rates of proteins in various tissues of Japanese quail. Int. J. Biochem. 23 (1991) 1005-1012.
5. [5] A.Y. Deutch, D.L. Rosin, M. Goldstein, R.H. Roth, 3-Acetylpyridine degeneration of the nigrostriatal dopamine system: an animal model of olivoponto-cerebellar atrophy-associated parkinsonism, Exp. Neurol. 105 (1989) 1-9.
6. [6] Z. Gottesfeld, F. Fonnum, Transmitter synthesizing enzymes in the hypoglossal nucleus and cerebellum: effect of acetylpyridine and surgical lesions, J. Neurochem. 28 (1977) 237-239.
7. [7] Y. Nakashima, R. Suzue, Effect of 3-acetylpyridine on the content of myelin in the developing rat brain, J. Nutr. Sci. Vitaminol. 30 (1984) 441-451.
8. [8] J.Y. Kim, S. Shin, I.K. Park, Effects of neurotoxin 3-acetylpyridine on levels of soluble proteins and enzyme activities in various tissues of Japanense quail, Int. J. Biochem. Cell Biol. 30 (1988) 487-495.
9. [9] S. Grisolia, The catalytic environment and its biological implications, Physiol. Rev. 44 (1964) 657-673.
10. [10] K.L. Lee, P.L. Darke, F.T. Kenney, Role of coenzyme in aminotransferase turnover, J. Biol. Chem. 252 (1977) 4958-4961.
11. [11] H. Inoue, H.C. Pitot, Regulation of the synthesis of serine dehydratase isozymes, Adv. Enz. Regul. 8 (1970) 289-296.
12. [12] J.W. Teipel, D.E. Koshland, Kinetic aspects of conformational changes in proteins. I. Rate of regain of enzyme activity from denatured proteins, Biochemistry 10 (1971) 792-798.
13. [13] I.K. Park, R.R. Marquardt, Effect of niacin deficiency on the thermal stability of NAD- and NADP-dependent dehydrogenases in liver and pectoral muscle of Japanese quail, Int. J. Biochem. Cell Biol. 28 (1996) 1169-1177.
14. [14] M. Klingenberg, in: H.U. Bergmeyer (Ed.), Methods of Enzymatic Analysis, vol. VII, Verlag Chimie Weinheim, Academic Press, New York, 1983.
15. [15] G.E. Glock, P. McLean, Further studies on the properties and assay of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver, Biochem. J. 55 (1953) 400-418.
16. [16] E.M. Wise Jr., E.G. Ball, Malic enzyme and lipogenesis, Proc. Natl. Acad. Sci. USA 52 (1964) 1255-1263.
17. [17] S.F. Velick, Glyceraldehyde-3-phosphate dehydrogenase, in: P.D. Boyer, H. Lardy, K. Myrback (Eds.), The Enzymes, vol. 7. Academic Press, New York, 1963, p. 243.
18. [18] Y. Hirota, E.M. Cohen, O.H.L. Bing, Lactate dehydrogenase and isoenzyme changes in rats with experimental thiamine deficiency, Metabolism 25 (1976) 1-8.
19. [19] G.L. Ellman, K.D. Courteny, V. Andres Jr., R.M. Featherstone, A new and rapid colorimetric determination of acetylcholinesterase activity, Biochem. Pharmacol. 7 (1961) 88-95.
20. [20] M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254.
21. [21] G.H. Smith, in: A Simplified Guide to Statistics, Holt, Reinhart and Winston, New York, 1962.
22. [22] J.Y. Kirn, I.K. Park, Effects of 6-aminonicotinamide on levels of soluble proteins and enzyme activities in various tissues of Japanense quail. Int. J. Biochem. Cell Biol. (1998) (in press).
23. [23] H.I. Kim, I.K. Park, Effect of prolonged starvation on the activities of muscle enzyme and acetylcholinesterase in tissues of Japanese quail, Int. J. Biochem. Cell Biol. 27 (1995) 1161-1168.
24. [24] I.K. Park, R.R. Marquardt, Effects of niacin deficiency on pyridine nucleotide levels and enzyme activities in various organs of young growing quail. J. Nutr. 112 (1982) 863-873.
25. [25] X.J. Ma, L.M. Salati, S.E. Ash, D.A. Mitchell, S.A. Klautky, D.A. Fantozzi, A.G. Goodridge, Nutritional regulation and tissue-specific expression of the malic enzyme gene in the chicken, J. Biol. Chem. 265 (1990) 18435-18441.
26. [26] I.R. Griffiths, P.A.T. Kelley, J.J. Grome, Glucose utilization in the central nervous system in the acute gliopathy due to 6-aminonicotinamide, Lab. Invest. 44 (1981) 547-552.
27. [27] Y.Z. Lin, S.J. Liang, J.M. Zhou, C.L. Tsou, P. Wu, Z. Zhou, Comparison of inactivation and conformational changes of D-glyceraldehyde dehydrogenase during thermal denaturation, Biochim. Biophys. Acta 1038 (1990) 247-252.
28. [28] Y.H. Koh, K.H. Choi, I.K. Park, Effects of niacin deficiency on the levels of soluble proteins and enzyme activities in various tissues of Japanese quail, Int. J. Biochem. Cell Biol. 30 (1998) 943-953.
29. [29] R. Rudolph, I. Heider, E. Westhof, R. Jaenicke, Mechanism of refolding and reactivation of lactic dehydrogenase from pig heart after dissociation in various solvent media, Biochemistry 16 (1977) 3384-3390.
30. [30] J. Massoulie, S. Bon, The molecular forms of cholinesterase and acetylcholinesterase in vertebrates, Annu. Rev. Neurosci. 5 (1982) 57-106.
31. [31] T. Skarzynski, A.J. Wonacott, Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus sterothermophilus. J. Mol. Biol. 23 (1988) 1097-1118.
32. [32] P.J. Marangos, S.M. Constantinides, Factors affecting the folding and association of flounder muscle glyceraldehyde-3-phosphate dehydrogenase, in vitro, Biochemistry 13 (1974) 904-910.