Rapid regulatory effect of tri-iodothyronine (T3) on antioxidant enzyme activities in a fish Anabas testudineus (Bloch): Short-term in vivo and in vitro study

Indian Journal of Biochemistry and Biophysics

Volumn 43, Issue 2, 2006, Pages 119-122

  Sreejith, P ^a   Oommen, O V ^a  

^a UNIVERSITY OF KERALA   (India)

Author keywords

Anabas testudineus; Antioxidant enzyme; Fish; Free radicals; Lipid peroxidation; Thyroid; Tri iodothyronine

Indexed keywords

ANTIOXIDANT; CATALASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; LIOTHYRONINE; SUPEROXIDE DISMUTASE;

ANIMAL; ARTICLE; ENZYME ACTIVATION; METABOLISM; PERCH; PHYSIOLOGY;

ANIMALS; ANTIOXIDANTS; CATALASE; ENZYME ACTIVATION; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; PERCHES; SUPEROXIDE DISMUTASE; TRIIODOTHYRONINE;

ANABAS TESTUDINEUS; TELEOSTEI;

EID: 33749162527     PISSN: 03011208     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (36)

1. Soboll S (1993a) Biochem Soc Trans 21, 799-803
2. Eales J G & Brown S B (1993) Rev Fish Biol Fisheries 3, 299-347
3. Leary S C, Barton K N & Ballantyne S (1996) Gen Comp Endocrinol 1104, 61-66
4. Soboll S (1993b) Biochim Biophys Acta 1144, 1-16
5. Ballantyne J S, John T M, Singer T D & Oommen O V (1992) J Exp Zool 261, 105-109
6. Battersby B J, McFarlane W J & Ballantyne J S (1996) J Exp Zool 274, 157-162
7. Bres O & Eales J G (1986) Gen Comp Endocrinol 61, 29-39
8. Das K & Chainy G B N (2001) Biochim Biophys Acta 1537, 1-13
9. Hogg N & Kalyanaraman B (1999) Biochim Biophvs Acta 1411, 378-384
10. Halliwell B & Gutteridge J M C (1985) Free Radicals in Biology and Medicine, pp. 542, Clarendon Press, Oxford
11. Peter M C S & Oommen O V (1993) J Exp Zool 266, 85-91
12. Verhoeven A J, Kamer P, Groen K & Tager J M (1985) J Biochem 226, 183-192
13. Otto M E & Moon T W (1996) Arch Environ Contam Toxicol 31, 141-147
14. Varghese S, Shameena B & Oommen O V (2001) Comp Biochem Physiol 128B, 165-171
15. Hardy R (1980) Fish feed formulation, FAO/UNDP Training Course in Fish Feed Technology, Seattle, pp. 233-240.
16. Slater C H & Schreck C B (1997) Gen Comp Endocrinol 106, 113-119
17. Sunny F, Lakshmy, P S & Oommen O V (2002) Comp Biochem Physiol 131, 297-304
18. Nichans W G & Samuelsson B (1968) Eur J Biochem 6, 126-130
19. Recknagel R O & Ghoshal A K (1966) Exp Mol Pathol 5, 413-426
20. Kakkar P, Das B & Viswanathan P N (1984) Indian J Biochem Biophys 21, 130-132
21. Lawrence R A & Burk R E (1976) Biochim Biophys Res Commun 17, 952-958
22. David M & Richard J S (1983) Method Enzymol Anal 3, 258-265
23. Maehly A & Chance B (1954) Methods of Biochem Anal 1, 357-424
24. Benke G M & Cheevar K C (1974) Toxicol Appl Pharmacol 28, 97-109
25. Lowry O H, Rosebrough N J, Farr A L & Randall R J (1951) J Biol Chem 193, 265-275
26. Duncan D B (1955) Biometrics 11, 1-42
27. Castilho R F, Zowaltowski A J & Vercesi A E (1998) Arch Biochem Biophys 345, 151-157
28. Nagyova A, Krajcovicova-kudlackova M, Horska A, Smolkova B, Blazicek Raslova, K, Collins A & Dusinska M (2004) Bratisl Lek Listy 105, 277-280
29. Karbownik M & Lewinski A (2003) Neuroendocrinol Lett 24, 293-303
30. Horton A A & Fairhurst S (1987) in Critical Reviews in Toxicology (Golberg L, ed), pp. 27-77, CRC Press, Inc, Florida
31. Seymen H O, Seven A, Civelek S, Yigit G, Hatemi H & Burcak G J (1999) J Basic Clin Physiol Pharmacol 10, 315-325
32. Chattopadhyay S, Zaidi G, Das K & Chainy G B N (2003) Indian J Exp Biol 41, 846-849
33. Komosinka-Vassev K, Olczyk K, Kucharz E J, Marcisz C. Winsz-Szczotka K & Kotulska A (2000) Clin Chim Acta 300, 107-117
34. Dhingra S, Singh U & Bansal M P (2003) Indian J Biochem Biophys 40, 265-273
35. Takahashi K, Newburger P E & Cohen H J (1986) J Clin Invest 77, 1402-1404
36. Morini P, Casalino E, Sblano C & Landriscina C (1991) Int J Biochem 23, 1025-1030