Thiamine triphosphate hydrolysis in non-excitable tissues: Purification and properties of thiamine triphosphatase from bovine kidney

Journal of Biochemistry, Molecular Biology and Biophysics

Volumn 5, Issue 1, 2001, Pages 75-82

  Makarchikov, Alexander F ^a  

^a INSTITUTE OF BIOCHEMISTRY   (Belarus)

Author keywords

Bovine kidney; Properties; Purification; Thiamine triphosphatase

Indexed keywords

4 NITROPHENYL PHOSPHATE; CALCIUM ION; COCARBOXYLASE; INOSINE PHOSPHATE; MAGNESIUM ION; MANGANESE; THIAMINE PHOSPHATE; THIAMINE TRIPHOSPHATASE; THIAMINE TRIPHOSPHATE;

ANIMAL TISSUE; ARTICLE; CALCULATION; CATTLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENERGY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; FRACTIONATION; GEL FILTRATION CHROMATOGRAPHY; HYDROLYSIS; KIDNEY; MOLECULAR WEIGHT; NONHUMAN; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN STRUCTURE; SOLUBILITY; TEMPERATURE; TISSUE;

EID: 0035761706     PISSN: 10258140     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (28)

1. Egi, Y., Koyama, S., Shikata, H., Yamada, K., Takashi, K. Content of thiamin phosphate esters in mammalian tissues. An extremely high concentration of thiamin triphosphate in pig skeletal muscle. Biochem. Int. 1986; 12: 385-390.
2. Cooper, J.R., Pincus, J.H. The role of thiamine in the nervous tissue. Neurochem. Res. 1979; 4: 223-239.
3. Nishino, K., Itokawa, Y., Nishino, N., Piros, K., Cooper, J.R. Enzyme system involved in the synthesis of thiamine triphosphate. I. Purification and characterization of protein-bound thiamine diphosphate: ATP phosphoryltransferase. J. Biol. Chem. 1983; 258: 11871-11878.
4. Cooper, J.R., Ruenwongsa, P. The role of bound thiamine pyrophosphate in the synthesis of thiamine triphosphate in rat liver. Biochim. Biophys. Acta. 1977; 482: 64-70.
5. Shikata, H., Koyama, S., Egi, Y., Yamada, K., Kawasaki, T. Cytosolic adenylate kinase catalyzes the synthesis of thiamin triphosphate from thiamin diphosphate. Biochem. Int. 1989; 18: 933-941.
6. Voskoboyev, A.I., Chernikevich, I.P., Luchko, V.S. Studies on thiamine diphosphate kinase (E.C. 2.7.4.15) from brewer's yeast: purification and some properties. Biomed. Biochim. Acta 1987; 46: 3-13.
7. Hashitani, Y., Cooper, J.R. The partial purification of thiamine triphosphatase from rat brain. J. Biol. Chem. 1972; 247: 2117-2119.
8. Barchi, R.L., Braun, P.E. A membrane-associated thiamine triphosphatase from rat brain. Properties of the enzyme. J. Biol. Chem. 1972; 247: 7668-7673.
9. Barchi, R.L., Viale, R.O. Membrane-associated thiamine triphosphatase. II. Activation by divalent cations. J. Biol. Chem. 1976; 251: 193-197.
10. Matsuda, T., Tonomura, H., Baba, A., Iwata, H. Membrane-associated thiamine triphosphatase in rat skeletal muscle. Int. J. Biochem. 1991; 23: 1111-1114.
11. Bettendorff, L., Wins, P., Schoffeniels, E. Thiamine triphosphatase from Electrophorus electric organ is anion dependent and irreversibly inhibited by 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid. Biochem. Biophys. Res. Commun. 1988; 154: 942-947.
12. Makarchikov, A.F., Chernikevich, I.P. Purification and characterization of thiamine triphosphatase from bovine brain. Biochim. Biophys. Acta 1992; 1117: 326-332.
13. Chernikevich, I.P., Gritsenko, E.A., Makarchikov, A.F., Voskoboev, A.I. An enzymatic micromethod for quantification of thiamine biphosphate in biological liquids. Prikl. Biokhim. Mikrobiol. 1991; 27: 762-771.
14. Sapry, M.K., Geetha, H., Shetty, T.K. A single reagent method of phosphate estimation in phosphatase(s) assay. Ind. J. Biochem. Biophys. 1987; 24: 340-343.
15. Weber, K., Osborn, M. The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. J. Biol. Chem. 1969; 244: 4406-4412.
16. Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 1976; 72: 248-254.
17. Penttinen, H.K., Uotila, L. The relation of the soluble thiamine triphosphatase activity of various rat tissues to nonspecific phosphatases. Med. Biol. 1981; 59: 177-184.
18. Chernikevich, I.P., Makarchikov, A.F. Cytosolic thiamine triphosphatase from bovine brain: 2. Interaction of thiamine triphosphate ester with the enzyme. Ukr. Biokhim. Zh. 1998; 70: 24-32.
19. Makarchikov, A.F., Chernikevich, I.P. Thiamine triphosphatase activity in bovine kidney. Biochem. Mol. Biol. Int. 1998; 46: 115-123.
20. Ferdinand, W. The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase. Biochem. J. 1966; 98: 278-283.
21. Itokawa, Y., Schulz, R.A., Cooper, J.R. Thiamine in nerve membranes. Biochim. Biophys. Acta 1972; 266: 293-299.
22. Matsuda, T., Tonomura, H., Baba, A., Iwata, H. Tissue difference in cellular localization of thiamine phosphate esters. Comp. Biochem. Physiol. 1989; 94B: 405-409.
23. Ogawa, K., Ago, Y., Tanaka, T. Ultrastructural cytochemistry of phosphatases related to thiamine metabolism. In: Gubler C.J., Fujiwara M. and Dreufus P.M., Eds. Thiamine. New York: John Wiley & Sons, 1976: 179-190.
24. Ogawa, K., Sakai, M., Inomata, K. Recent findings on ultra-cytochemistry of thiamin phosphatases. Ann. NY Acad. Sci. 1982; 378: 188-214.
25. Itokawa, Y., Cooper J.R. Thiamine release from nerve membranes by tetrodotoxin. Science 1969; 166: 759-761.
26. Doegre, D.R., McNamee, M.G., Ingraham, L.L. Some neurochemical properties of thiamin. Ann. NY Acad. Sci. 1982; 378: 422-434.
27. Bettendorff, L. Thiamine in excitable tissues: reflections on a non-cofactor role. Metab. Brain Dis. 1994; 9: 183-209.
28. Franciolini, F., Petris, A. Chloride channels of biological membranes. Biochim. Biophys. Acta 1990; 1031: 247-259.