Purification and properties of thioltransferase from monkey small intestinal mucosa: Its role in protein-s-thiolation

International Journal of Biochemistry and Cell Biology

Volumn 28, Issue 9, 1996, Pages 1051-1059

  Benard, O ^a   Balasubramanian, K A ^a  

^a CHRISTIAN MEDICAL COLLEGE   (India)

Author keywords

Monkey intestinal mucosa; Protein s thiolation; Thiol disulfide exchange activity; Thioltransferase

Indexed keywords

THIOL; TRANSFERASE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INTESTINE MUCOSA; MOLECULAR WEIGHT; MONKEY; NONHUMAN; OXIDATIVE STRESS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN PROCESSING;

ANIMALIA;

EID: 0030250901     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/1357-2725(96)00031-3     Document Type: Article

References (34)

1. Ahamed A., Surolia A. and Bacchwaat B. K. (1977) Affinity chromatographic separation of arylsulfatase A and B using Cibacron blue Sepharose. Biochem. Biophys. Acta. 481, 542-548.
2. Axelsson K., Eriksson S. and Mannervik B. (1978) Purification and characterisation of cytoplasmic thioltransferase (glutathione : disulfide oxidoreductase) from rat liver. Biochemistry 17, 2978-2984.
3. Benard O. and Balasubramanian K. A. (1993) Effect of oxidant exposure on thiol status in the intestinal mucosa. Biochem. Pharmacol. 45, 2011-2015.
4. Benard O. and Balasubramaninan K. A. (1995) Effect of oxidised glutathione on intestinal mitochondria and brush border membrane. Int. J. Biochem. Cell Biol. 27, 589-595.
5. Carlberg I. and Mannervik B. (1985) Glutathione reductase. Meth. Enzymol. 113, 484-490.
6. Carmichel D. F., Morin J. E. and Dixon J. E. (1977) Purification and characterisation of thiol : protein disulfide oxidoreductase from bovine liver. J. biol. Chem. 252, 7163-7167.
7. Fariss M. W. and Reed D. J. (1987) High performance liquid chromatography of thiols and disulfides: dinitrophenol derivaties. Meth. Enzymol. 143, 101-109.
8. Gan Z. and Wells W. W. (1988) Purification and properties of thioltransferase. J. biol. Chem. 261, 996-1001.
9. Hatakayama M., Tanimoto Y. and Mizoguchi T. (1984) Purification and some properties of bovine liver cytosol thioltransferase. J. Biochem. 95, 1811-1818.
10. Hatakayama M., Lee C., Chary C., Hayashi M. and Mizoguchi T. (1985) Release of thioltransferase from rabbit polymorphonuclear leucocytes by immune complex in vitro and inhibition of the enzyme by chloramphenicol. Biochem. Biophys. Res. Commun. 127, 458-463.
11. Hopper S., Johnson R. S., Vathi J. E. and Biemann K. (1989) Glutaredoxin from rabbit bone marrow. Purification, characterisation and amino acid sequence determination by tandem mass spectrometry. J. biol. Chem. 264, 20438-20447.
12. Holmgren A. (1989) Thioredoxin and glutaredoxin systems. J. biol. Chem. 264, 13963-13966.
13. Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
14. Larson K., Eriksson V. and Mannervik B. (1985) Thioltransferase from human placenta. Meth. Enzymol. 113, 520-524.
15. Livesay J. L. and Reed D. J. (1984) Measurement of glutathione protein mixed disulfides. Int. J. Radiat. Oncol. Biol. phys. 10, 1507-1510.
16. Lowry O. H., Rosebrough N., Farr A. L. and Randall R. J. (1951) Protein measurement with the Folin-phenol reagent. J. biol. Chem. 193, 265-275.
17. Mannervik B., Persson G. and Eriksson S. (1974) Enzymatic catalysis of the reversible sulfitolysis of glutathione disulfide and the biological reduction of thiosulfate esters. Arch. Biochem. Biophys. 163, 283-289.
18. Mannervik B. and Axelsson K. (1975) Reduction of disulfide bonds in protein and protein mixed disulfides catalysed by a thioltransferase in rat liver cytosol. Biochem. J. 149, 785-788.
19. Mannervik B., Axelsson K. and Larson K. (1981) Thioltransferase.. Meth. Enzymol. 77, 281-285.
20. Mannervik B., Axelsson K., Sunderwall A. C. and Holmgren A. (1983) Relative contribution of thioltransferase and thioredoxin dependent systems in reduction of low molecular mass and protein disulfide. Biochem. J. 213, 519-523.
21. McKernan T. B., Woods E. B. and Lash L. H. (1991) Uptake of glutathione by renal cortical mitochondria. Arch Biochem Biophys. 288, 653-663.
22. Mieyal J. J., Starke D. W., Gravina S. A., Dothey C. and Chung J. S. (1991) Thioltransferase in human red blood cells: purification and properties. Biochemistry 30, 6088-6097.
23. Miller R. M., Park E. M. and Thomas J. A. (1991) Reduction (dethiolation) of protein mixed-disulfides: distribution and specificity of dethiolating enzymes and N,N′-bis(2-chloroethyl)-N-nitrosourea inhibition of an NADPH-dependent cardiac dethiolase. Arch. Biochem. Biophys. 287, 112-120.
24. +)-EDTA-mediated oxidative stress. Biol. Pharm. Bull. 17, 607-611.
25. Mizoguchi T., Nishinaka T., Nanjo H., Yagi K. and Hakusui H. (1995) Modulation of subcellular particles of the rat small intestine and liver by ebselen. Biol. Pharm. Bull. 18, 491-495.
26. Moutiez M., Aumercier M., Schoneck R., Meziane-Cherif P., Lucas V., Aumercier P., Quaissi A., Sergherarert C. and Tartar A. (1985) Purification and characterization of a trypanothione-glutathione thioltransferase from Trypanasoma cruzi. Biochem. J. 310, 433-437.
27. Nagai S. and Simon B. (1968) A thiol-disulfide transhydrogenase from yeast. J. biol. Chem. 243, 1942-1947.
28. Ravindranath V. and Reed D. J. (1990) Glutathione depletion and formation of protein mixed disulfide following exposure of brain mitochondria to oxidative stress. Biochem. Biophys. Res. Commun. 169, 1075-1079.
29. Schuppe-Koistinen I., Gerdes R., Moldeus P. and Cotgreave I. A. (1994) Studies on the reversibility of protein s-thiolation in human endothelial cells. Arch. Biochem. Biophys. 315, 226-234.
30. Terada T., Maeda H., Okamoto K., Nishinaka T., Mizoguchi T. and Nishihara T. (1993) Modulation of glutathione s-transferase activity by a thiol/disulfide exchange reaction and involvement of thioltransferase. Arch. Biochem. Biophys. 300, 495-500.
31. Turren J. F. and Boveris A. (1980) Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191, 421-427.
32. Turrens J. F., Alexandre A. and Lehninger A. L. (1985) Ubisemiquinone is the electron donor for superoxide anion formation. Arch. Biochem. Biophys. 237, 408-411.
33. Weber K. and Osborn M. (1965) The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. J. biol. Chem. 244, 4406-4412.
34. Ziegler D. M. (1985) Role of reversible oxidation-reduction of enzyme thiol-disulfides in metabolic regulation. Annu. Rev. Biochem. 54, 305-329.