Skip to main content
Log in

Alterations in enzymes in an Indian catfish, Clarias batrachus (Linn.), exposed to vanadium

  • Published:
Bulletin of Environmental Contamination and Toxicology Aims and scope Submit manuscript

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

References

  • Andersson T, Pesonen M, Johansson C (1985) Differential induction of cytochrome P-450 dependent monoxygenase, epoxide hydrolase. glutathione transferase and UDP glucuronosyl transferase activities in the liver of rainbow trout by β-naphthoflavone or Clophen A50. Biochem Pharmacol 34: 3309–3314

    Google Scholar 

  • Castuma CE, Brenner RR (1989) The influence of fatty acid unsaturation and physical properties of microsomal membrane phospholipids on UDP-glucuronyl transferase activity. Biochem J 258: 723–731

    Google Scholar 

  • Conney AH (1982) Induction of microsomal enzymes by foreign chemicals and carcinogenesis by polycyclic aromatic hydrocarbons. Cancer Res 42: 4875–4917

    Google Scholar 

  • Dekant W, Lash LH, Anders MW (1987) Bioactivation mechanism of the cytotoxic and nephrotoxic S-Conjugate S-(2-chlor-l,l,2-trifluoroethyl)-L-Cysteine. Proc Natl Acad Sci 84: 7443–7447

    Google Scholar 

  • Dierickx PJ (1982) In vitro inhibition of the soluble glutathioneS-transferase from rat liver by heavy metals. Enzyme 27: 25–32

    Google Scholar 

  • Förlin L, Haux C (1985) Increased excretion in the bile of 17B(3H) estradiol-derived radioactivity in rainbow trout treated with β-naphthoflavone. Aquat Toxicol 6: 197–208

    Google Scholar 

  • Gooch JW, Matsumara F (1983) Characteristics of the hepatic monoxygenase system of the goldfish (Carassino auratus) and its induction with β-naphthoflavone. Toxicol Appl Pharmacol 68: 380–391

    Google Scholar 

  • Habig WH, Pabst MJ, Jacoby WB (1974) Glutathione-S-transferase, the first enzymatic step in mercapturic acid formation. J Biol Chem 251: 7130–7139

    Google Scholar 

  • Haider SS, Elfakhri M (1991) Action of a tocopherol on vanadium stimulated lipid peroxidation in rat brain. Neurotoxicol 12: 79–87

    Google Scholar 

  • Hardwick JP, Song B-J, Huberman E, Gonzalez FJ (1987) Isolation, complementary DNA sequence, and regulation of rat hepatic lauric acid ω-hydroxylase (Cytochrome P-450LA ω). J Biol Chem 262: 801–810

    Google Scholar 

  • Holdway DA, Sprague JB (1979) Chronic toxicity of vanadium to flagfish. Wat Res 13: 905–910

    Google Scholar 

  • Jandhyala BS, Hom GJ (1983) Physiological and pharmacological properties of vanadium. Life Sci 33: 1325–1340

    Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RL (1951) Protein measurements with the folinphenol reagent. J Biol Chem 193: 265–275

    CAS  PubMed  Google Scholar 

  • Merill JC, Bray TM (1982) The effect of dietary protein on the activity of UDP-glucuronyl transferase and its physiological significance in drug metabolism. Can J Physiol Pharmacol 60: 1556–1561

    Google Scholar 

  • Miramand P, Fowler SW, Guary JC (1992) Experimental study on vanadium transfer in the benthic fish Gobius minutus. Mar Biol 114: 349–353

    Google Scholar 

  • Neuman CM, Zannoni VG (1990) Ascorbic acid deficiency and hepatic UDP-glucuronyl transferase. Qualitative and quantitative difference. Biochem Pharmacol 39: 1085–1093

    Google Scholar 

  • Omura T, Sato R (1964) The carbon monoxide binding pigment of liver microsomes, I and II. J Biol Chem 239: 2370–2385

    Google Scholar 

  • Payne JF, Fancey LL, Rahimtula AD, Porter EL (1987) Review and perspective on the use of mixed-function oxygenase enzymes in biological monitoring. Comp Biochem Physiol 86C: 233–245

    Google Scholar 

  • Sato K (1990) Glutathione transferase as markers of preneoplasia and neoplasia. Adv Cancer Res 52: 205–255

    Google Scholar 

  • Vodicnik MJ, Elcombe CE, Lech JJ (1981) The effect of various types of inducing agents on hepatic microsomal monoxygenase activity in rainbow trout. Toxicol Appl Pharmacol 59: 364–374

    Google Scholar 

  • Zhang YS, Andersson T, Förlin L (1990) Induction of hepatic xenobiotic biotransformation enzymes in rainbow trout by β-naphthoflavone. Time course studies. Comp Biochem Physiol 95B: 247–253

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Chakraborty, A., Bhattacharjee, S. & Chatterjee, M. Alterations in enzymes in an Indian catfish, Clarias batrachus (Linn.), exposed to vanadium. Bull. Environ. Contam. Toxicol. 54, 281–288 (1995). https://doi.org/10.1007/BF00197442

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00197442

Keywords

Navigation