Enzyme-Linked Immunosorbent Assay for Metal-Binding Proteins of Mytilus Edulis

  • G. Roesijadi
  • J. E. Morris
Part of the Lecture Notes on Coastal and Estuarine Studies book series (COASTAL, volume 25)


Metallothioneins (MTs) are cysteine-rich, low molecular weight, metal-binding proteins whose functions, although not clearly understood, appear to be involved with detoxification, storage, and regulation of copper, zinc, cadmium, and mercury (reviews by Webb, 1979; Cousins, 1985). These proteins have been detected in diverse organisms and are ubiquitously distributed in the animal kingdom (Kojima and Kagi, 1978; Roesijadi, 1981; Klaaverkamp et al., 1984), as well as in some fungi (Hamer et al., 1985) and prokaryotes (Olafson et al., 1980). In numerous studies, marine and freshwater fish and invertebrates have been shown capable of synthesizing increased levels of MT’s or similar proteins in response to metal exposure.


Mytilus Edulis Chesapeake Biological Laboratory Metallothionein Induction Dynatech Laboratory Tissue Mercury Concentration 
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  1. Cousins, R.J. 1985. Absorption, transport, and hepatic metabolism of copper and zinc: special reference to metallothionein and ceruloplasmin. Physiol. Rev. 65: 238–309.PubMedGoogle Scholar
  2. Garvey, J.S., R.J. Vander Mallie and C.C. Chang. 1982. Radio immunoassay of metallothioneins. IN: Methods in Enzymology. J.J. Langone and H. Van Vunakis (eds.). Academic Press, NY. pp. 121–138.Google Scholar
  3. George, S.G. and B.J.S. Pirie. 1980. Metabolism of zinc in the mussel, Mytilus edulis (L.): a combined ultrastructural and biochemical study. J.Mar. Biol. Ass. U.K. 60: 575–590.CrossRefGoogle Scholar
  4. Hamer, D.H., D.J. Thiele and J.E Lemontt. 1985. Function and autoregulation of yeast copperthionein. Science. 228: 685–690.PubMedCrossRefGoogle Scholar
  5. Klaaverkamp, J.F., W.A. Macdonald, D.A. Duncan and R. Wagemann. 1984. Metallothionein and acclimation heavy metals in fish: a review. IN: Contaminant Effects on Fisheries. V.W. Cairns, P.V. Hodson and J.O Nriagu. (eds.). John Wiley and Sons, Inc. pp. 100–113.Google Scholar
  6. Kogima, Y. and J.H.R. Kagi. 1978. Metallothionein. Trends Biochem. Sci. 3: 89–94.Google Scholar
  7. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.PubMedCrossRefGoogle Scholar
  8. Olafson, R.W., S. Loya and R.G. Sim. 1980. Physiological parameters of prokaryotic metallothionein induction. Biochem. Biophys. Res. Comm. 95: 1495–1503.PubMedCrossRefGoogle Scholar
  9. Roch, M., J.A. McCarter, A.T. Matheson, M.J.R. Clark and R.W. Olafson. 1982. Hepatic metallothionein induction in rainbow trout (Salmo gairdneri) as an indicator of metal pollution in the Campbell River System. Can. J. Fish. Aquatic. Sci. 19: 1596–1601.CrossRefGoogle Scholar
  10. Roesijadi, G. 1981. The significance of low molecular weight, metallothionein-like proteins in marine invertebrates: current status. Mar. Environ. Res. 4: 167–179.CrossRefGoogle Scholar
  11. Roesijadi, G. 1982. Uptake and incorporation of mercury into mercury-binding proteins of gills of Mytilus edulis as a function of time. Mar. Biol. 66: 151–157.CrossRefGoogle Scholar
  12. Roesijadi, G. and A.S. Drum. 1982. Influence of meracaptoethanol on the isolation of mercury-binding proteins from the gills of Mytilus edulis. Comp. Biochem. Physiol. 71B: 455–459.Google Scholar
  13. Signorella, A.P. and W.C. Hymer. 1984. An enzyme-linked immunosorbent assay for rat prolactin. Anal. Biochem. 136: 372–381.PubMedCrossRefGoogle Scholar
  14. Viarengo, A., M. Pertica, G. Mancinelli, S. Palermero, G. Zanicchi and M. Orunesu. 1981. Synthesis of Cu-binding proteins in different tissues of mussels exposed to the metal. Mar. Bull. Pollut. 12: 347–350.CrossRefGoogle Scholar
  15. Voller, A., D.E. Bidwell and A. Bartlett. 1979. The Enzyme Linked Immunosorbent Assay. Dynatech Laboratories, Inc., Alexandria. 125 pp.Google Scholar
  16. Waalkes, M.P., J.S. Garvey and C.D. Klaasen. 1985. Comparison of methods of metallothionein quantification: cadmium radioassay, mercury radioassay, and radioimmunoassay. Toxicol. Appli. Pharmacol. 79: 524–527.CrossRefGoogle Scholar
  17. Webb, M. 1979. The metallothioneins. IN: The Chemistry, Biochemistry, and Biology of Cadmium. M. Webb (ed.). Elsevier North-Holland Biomedical Press, NY. pp. 195–266.Google Scholar

Copyright information

© Springer-Verlag New York, Inc. 1988

Authors and Affiliations

  • G. Roesijadi
    • 1
  • J. E. Morris
    • 2
  1. 1.Department of BiologyPennsylvania State UniversityUniversity ParkUSA
  2. 2.Battelle, Pacific Northwest LaboratoryBiology and Chemistry DepartmentRichlandUSA

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