Skip to main content

Toxicokinetic study of rat intestinal brush border membrane enzymes following in vitro exposure to lead and vanadium

This is a preview of subscription content, access via your institution.

References

  1. Boelsterli U, Zbinden G (1979) Application of fine needle aspiration biopsy for the diagnosis of dysplastic and neoplastic liver cell changes induced by N-nitrosomorpholine in rats. Arch Toxicol 42:225–233.

    Google Scholar 

  2. Bond GH, Hudgins PM (1980) Inhibition of red cell Ca+2-ATPase by vanadate. Biochim Biophys Acta 600:781–790.

    Google Scholar 

  3. Cantley LC (Jr), Cantley LG, Hosephson L (1978) A characterization of vanadate interactions with (Na+ +K+)ATPase, mechanistic and regulatory implication. J Biol Chem 253:7361–7368.

    Google Scholar 

  4. Dahlqvist A (1964) Methods for the assay of intestinal disaccharidases. Anal Biochem 7:18–25.

    Google Scholar 

  5. Dixon M (1953) Determination of enzyme inhibitor constants. Biochem J 55:170–171.

    Google Scholar 

  6. Dux L, Martonosi A (1983) Ca+2-ATPase crystals in sarcoplasmic reticulum: Effect of trypsin digestion. J Biol Chem 258:10111–10115.

    Google Scholar 

  7. Forstner GG, Sebesin SM, Isselbacker KJ (1968) Rat intestinal microvillus membranes. Biochem J 106:381–390.

    Google Scholar 

  8. Goldstein GW, Ar D(1983) Lead activated calmodulin sensitive processes. Life Sci 33:101–106.

    Google Scholar 

  9. Haffar JJ, Rowe NA, Tomicic TK (1988) The non specific nature of the vanadate inhibition of rat ileal Na+-K+-ATPase. Life Sci 43:1741–1746.

    Google Scholar 

  10. Hestrin S (1949) Reaction of acetylcholine and other carboxylic acid derivatives with hydroxylamine. J Biol Chem 180:249–261.

    Google Scholar 

  11. Hidalgo C, Gonzalez ME, Logos R (1983) Characterization of Ca+2 or Mg+2-ATPase of transverse tubule membranes isolated from rabbit skeletal muscle. J Biol Chem 258:13937–13945.

    Google Scholar 

  12. Holtzman D, Hus JS, Mortell P (1978) In vitro effects of inorganic lead on isolated rat brain mitochondrial respiration. Neurochem Res 3:195–200.

    Google Scholar 

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

    Google Scholar 

  14. Klip A, Grinstein S, Semenza G (1979) Transmembrane disposition of the phlorizin binding protein of intestinal brush border. FEBS Lett 99:91–96.

    Google Scholar 

  15. Kuliszewska KT, Nicholis DM (1985) Rat kidney brush border enzyme activity following subchronic oral exposure. Toxicol Appl Pharmacol 77:211–218.

    Google Scholar 

  16. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with folin phenol reagent J Biol Chem 193:265–275.

    CAS  PubMed  Google Scholar 

  17. Nordberg GF (1976) In: Effect and dose response relationship of toxic metals. Elsevier Scientific Pub. Co. New York: p15.

    Google Scholar 

  18. Pirkle JL, Shwartz J, Landis JR, Harlen WR (1985) The relationship between blood lead level and blood presure and its cardiovascular risk implications. Amer J Epidemiol 121:246–258.

    Google Scholar 

  19. Siegel, GJ, Fogt SK (1977) Inhibition by lead ion of electrophorus Na+ -K+ -adenosine triphosphatase and K+-p-nitrophenyl phosphatase. J Biol Chem 252:5201–5205.

    Google Scholar 

  20. Weiser MM (1973) Intestinal cell surface membrane glycoprotein synthesis — An indicator of cellular differentiation. J Biol Chem 248:2536–2541.

    Google Scholar 

Download references

Author information

Affiliations

Authors

Corresponding author

Correspondence to A. M. Kidwai.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Gupta, K., Upreti, R.K. & Kidwai, A.M. Toxicokinetic study of rat intestinal brush border membrane enzymes following in vitro exposure to lead and vanadium. Bull. Environ. Contam. Toxicol. 52, 919–926 (1994). https://doi.org/10.1007/BF00200703

Download citation

Keywords

  • Enzyme
  • Waste Water
  • Vanadium
  • Water Management
  • Water Pollution