Isolation and properties of cytoplasmic α-glycerol 3-phosphate dehydrogenase from the pectoral muscle of the fruit bat, Eidolon helvum

Journal of Biochemistry and Molecular Biology

Volumn 36, Issue 2, 2003, Pages 159-166

  Agboola, Femi Kayode ^a   Thomson, Alan ^b   Afolayan, Adeyinka ^a  

^a OBAFEMI AWOLOWO UNIVERSITY   (Nigeria)

^b LANCASTER UNIVERSITY   (United Kingdom)

Author keywords

Animal bat flight; Fruit bat; Glycerol 3 phosphate dehydrogenase; Pectoral breast muscle

Indexed keywords

ANIMALIA; EIDOLON HELVUM;

EID: 12844262009     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: 10.5483/bmbrep.2003.36.2.159     Document Type: Article

References (44)

1. Afolayan, A. (1989) The essential cysteine of Candida utilis glucose-6-phosphate dehydrogenase. Nig. J. Natl. Sci. 4, 61-65.
2. Balmfort, A. J. (1982) Production, purification and characterization of glyoxylate dehydrogenase from Sclerotium rolfsii (Sacc). Ph.D. Thesis, Lancaster University, Lancaster, U.K; 1982.
3. Bennakkers, A. M. T. (1969) Carbohydrates and fat as a fuel for insect flight: A comparative study. J. Insect Physiol 15, 353-361.
4. Brosemer, R. W. and Marquart, R. R. (1966) Insect extramitochondrial glycerophosphate dehydrogenase: II. Enzymic properties and amino acid composition of the enzyme from honey bee (Appis mellifera) Thoraces. Biochem. Biophys. Acta 128, 464-473.
5. Chance, B. and Sacktor, B. (1958) Respiratory metabolism of insect flight muscle: II Kinetic of respiratory enzymes in flight muscle sarcosomes. Archs. Biochem. Biophys. 76, 509-531.
6. Degani, Y. and Degani, C. (1979) Subunit selective chemical modifications of creatine kinase. Evidence for asymmetrical associations of the subunits. Biochem. 15, 5917-5923.
7. Dixon, M. (1953) The determination of enzyme inhibitor constants. Biochem. J. 55, 170-171.
8. Florini, J. R. and Vestling, C. S. (1951) Graphical determination of the dissociation constants from two substrate enzyme system. Biochem. Biophys. Acta 25, 575-578.
9. Fondy, T. P., Herwig, K. J., Sollohub, S. J. and Rutherford, D. B. (1971) Isolation and structural properties of cytoplasmic glycerol-3-phosphate dehydrogenase from rat liver. Archs. Biochem. Biophys. 145, 583-590.
10. Fondy, T. P., Levin, L., Sollohub, S. J. and Ross, C. R. (1968) Structural studies on nicotinamide adenine dinucleotide linked L-α-glycerol-3-phosphate dehydrogenase crystallized from rat skeletal muscle. J. Biol Chem. 243, 3148-3160.
11. Fondy, T. P., Ross, C. R. and Sollohub, S. J. (1969) Structural studies on rabbit muscle glycerol-3-phosphate dehydrogenase and comparison of chemical and physical determinations of its molecular weights. J. Biol. Chem. 244, 1631-1644.
12. Fondy, T. P., Solomon, J. and Ross, C. R. (1971) Comparison of cytoplasmic glycerol-3-phosphate dehydrogenase from rat liver and muscle. Arch. Biochem. Biophys. 145, 601-611.
13. George, J. C. and Jyoti, D. C. (1955) Histological features of the breast and leg muscles of birds and bats and their physiological and evolutionary significance. J. Anim. Morph. Physiol. 11, 31-35.
14. Gilbert, I. L. (1967) Lipid metabolism and function in insect. Adv. Insect Physiol. 4, 64-211.
15. Gonzalez-Cerezo, H. and Dalziel, K. (1982) L-α-glycerophosphate dehydrogenase from beef liver. Methods Enzymol. Vol. XLI, Part B. 259-264.
16. Green, D. E. (1936) α-glycerophosphate dehydrogenase. Biochem. J. 30, 629-644.
17. Guppy, M. and Hochachka, P. W. (1978) Role of dehydrogenase competition in metabolic regulation, the case of lactase and α-glycerophosphate dehydrogenase. J. Biol. Chem. 253, 8465-8469.
18. Guppy, M. and Hochachka, P. W. (1978) Controlling the highest lactate dehydrogenase activity known in nature. Am. J. Physiol. 234, 2136-2140.
19. Gutierrez, M., de Burges, N. M. G., Burges, C. and Clanco, A. (1974) Correlation between muscular lactate dehydrogenase isozyme, patterns and flight habits of bats. Comp Biochem. Physiol. B.8, 379-388.
20. Holbrook, J., Liljas, A., Steindel, S. and Rossman, M. (1975) The Enzymes, Boyer, P. D., (ed.), Vol. II, Part A, Academic Press, New York, New York.
21. Klingenberg, M. and Bucher, T. H. (1960) Biological oxidations. Ann. Rev. Biochem. 29, 669-708.
22. Kito, M. and Pizer, L. I. (1969) Purification and regulatory properties of the biosynthetic L-glycerol-3-phosphate dehydrogenase from Escherichia colt. J. Biol. Chem. 244, 3316-3323.
23. Koekemoer, T. C., Litthauer, D. and Oelofson, H. J. (1995) Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase. Int. J. Biochem. Cell. Biol. 27, 625-632.
24. Kornbluth, R. A., Ostro, M. J., Rittman, L. S. and Fondy, T. P. (1974) Affinity chromatography of cytosolic NAD-linked glycerol-3-phosphate dehydrogenase from normal and neoplastic mammalian tissues. FEBS Lett. 39, 190-194.
25. Lee, Y. P. and Craine, J. E. (1971) L-glycerol 3-phosphate dehydrogenase: I. Effects of substrates on the catalytic properties of the hepatic nicotinamide adenine dinucleotide-linked enzyme from rabbit. J. Biol. Chem. 246, 7616-7622.
26. Lowry, D. H., Rosebrough, N. J., Fair, A. L. and Randell, R. J. (1951) Protein measurement with Folin phenol reagent. J. Biol. Chem. 193, 265-275.
27. Machado, M. F. and Contel, E. P. (1991) Glycerol-3-phosphate isoenzyme variation in adult meliponids (Hymeroptepron: Apidae). Biochem. Genet. 29, 93-600.
28. Marquart, R. R. and Brosemer, R. W. (1966) Insect extramitochondrial glycerophosphate dehydrogenase: Crystallization and physical properties of the enzyme from honey bee (Appis mellifera) Thoraces. Biochem. Biophys. Acta 128, 454-463.
29. McGinnins, J. F. and Vellis, J. (1974a) Purification and characterization of a rat brain glycerol phosphate dehydrogenase. Biochem. Biophys. Acta 364, 17-27.
30. McGinnis, J. F. and Vellis, J. A. (1974b) Novel affinity column for purification of glycerol phosphate dehydrogenase. Biochem. Biophys. Res. Commun. 60, 186-195.
31. Okon, E. E., Umukoro, R. M. and Ajudua, A. (1978) Diurnal variations of the glycogen and fat stores in the liver and breast muscle of fruit bat, Eidolon helvum (Kerr). Physiol. Behav. 20, 121-123.
32. +-linked glycerol-3-phosphate dehydrogenase from normal and neoplastic rabbit tissues. J. Biol. Chem. 252, 5575-5583.
33. Ratner, P. L., Fisher, M., Burkart, D., Cook, J. R. and Kozak, L. P. (1981) The role of mRNA levels and cellular localization in controlling sn-glycerol-3-phosphate dehydrogenase expression in tissue of the mouse. J. Biol. Chem. 256, 3576-3579.
34. Ross, C. R., Curry, S., Schwatz, A. W. and Fondy, T. P. (1971) Multiple molecular forms of cytoplasmic glycerol-3-phosphate dehydrogenase in rat liver. Arch. Biochem. Biophys. 145, 591-603.
35. Sacktor, B. (1965) Energetics and respiratory metabolism of muscular contraction (Rockstein, M., editor. The physiology of Insects,.), Vol. II, pp. 483-580, Academic Press, New York.
36. Sellinger, O. Z. and Miller, O. N. (1956) Anion inhibition of a-glycerophosphate dehydrogenase. Nature (London) 183, 889-890.
37. Thomas, S. P. (1975) Metabolism during flight in two species of bats, Phyllostomus hastatus and Pteropus gouldii. J. Exp. Biol. 63, 273-293.
38. Thomas, S. P. and Suther, R. A. (1972) The physiology and energetics of bat flight. J. Exp. Biol. 57, 317-335.
39. von Euler, H., Alder, E. and Gunther, G. (1937) The components of the dehydrase systems: XV. The dehydrogenation of α-glycerophosphoric acid in the animal body. Z. Physiol. Chemie 249, 1-17.
40. Warburg, O. and Christian, W. (1942) Isolierung and Crystallization des garungsferments enolase. Biochem. Z. 310, 384-421.
41. Warkentin, D. L. and Fondy, T. P. (1973) Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal adipose tissue and its comparison with skeletal muscle enzyme. Eur. J. Biochem. 36, 97-99.
42. Weber, K. and Osborn, M. (1975) Protein and sodium dodecyl sulphate. Molecular weight determination on polyacrylamide gels and related procedures: in The Proteins, Neurath, H. and Hill, R. L. (eds.), 3rd Ed., Vol. I., pp. 179-223, Academic Press, New York, New York.
43. White, H. B. and Kaplan, N. O. (1969) Purification and properties of two types of diphosphopyridine nucleotide linked glycerol-3-phosphate dehydrogenases from chicken muscle and chicken liver. J. Biol. Chem. 244, 6031-6039.
44. Zolnierowicz, S., Swiercynski, J. and Zelewski, L. (1986) Isolation and properties of glycerol-3-phosphate oxidoreductase from human placenta. Eur. J. Biochem. 154, 161-166.