Skip to main content
NCBI home page
Environmental Health Perspectives logoLink to Environmental Health Perspectives
. 1986 Mar;65:63–69. doi: 10.1289/ehp.866563

Purification and characterization studies of cadmium-binding proteins from the American oyster, Crassostrea virginica.

B A Fowler, D W Engel, M Brouwer
PMCID: PMC1474711  PMID: 3709468

Abstract

The previously reported low molecular weight cadmium-binding protein (CdBP) from the American oyster, Crassostrea virginica, has been further purified and characterized by improved technical methods. The internal organ distribution of the protein within the oyster and effects of life cycle/season on CdBP production also have been evaluated. CdBP isolated by extended ion-exchange gradients or double ion-exchange chromatography followed by HPLC analysis possesses an electrophoretic Rf of about 0.7 and contains relatively little Zn, as previously reported. Cysteine, lysine, and glycine are the dominant amino acids. When ion-exchange columns are developed with NaCl gradients, the aromatic residues tryptophan, tyrosine, and phenylalanine are found to be present, but these may be largely removed depending upon whether the protein is denatured and carboxymethylated prior to analysis. The ultraviolet absorption spectrum of CdBP also was variable, with 250/280 nm ratios ranging from 17:1 immediately after ion-exchange chromatography to 2:1 following concentration procedures. Internal organ distribution studies showed that the visceral mass contained most of the Cd present with lesser amounts in the gills and mantle. In contrast with mammals, CdBP accounts for only about 30% of the total cell Cd burden in these tissues. Cu displacement of Cd from the protein is a particular problem during the summer spawning season and appears to stem from altered Cu metabolism during this period. Relative oyster dormancy during the winter also reduces CdBP production in response to Cd, and the protein is obtained most readily during the fall and spring.(ABSTRACT TRUNCATED AT 250 WORDS)

Full text

PDF
63

Images in this article

67FIGURE 7.
on p.67

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bornmann L., Hess B., Zimmermann-Telschow H. Mechanism of renaturation of pyruvate kinase of Saccharomyces carlsbergensis: activation by L-valine and magnesium and manganese ions. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1525–1529. doi: 10.1073/pnas.71.4.1525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  3. Fowler B. A., Megginson M. M. Isolation and partial characterization of a high molecular weight Cd/Zn-binding protein from the kidney of the scallop Placopecten magellanicus: preliminary studies. Environ Health Perspect. 1986 Mar;65:199–203. doi: 10.1289/ehp.8665199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Frazier J. M. Cadmium-binding proteins in the mussel, Mytilus edulis. Environ Health Perspect. 1986 Mar;65:39–43. doi: 10.1289/ehp.866539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. George S. G., Carpene E., Coombs T. L., Overnell J., Youngson A. Characterisation of cadmium-binding proteins from mussels, Mytilus edulis (L), exposed to cadmium. Biochim Biophys Acta. 1979 Oct 24;580(2):225–233. doi: 10.1016/0005-2795(79)90135-1. [DOI] [PubMed] [Google Scholar]
  6. Kägi J. H., Vasák M., Lerch K., Gilg D. E., Hunziker P., Bernhard W. R., Good M. Structure of mammalian metallothionein. Environ Health Perspect. 1984 Mar;54:93–103. doi: 10.1289/ehp.54-1568188. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Nordberg M., Nuottaniemi I., Cherian M. G., Nordberg G. F., Kjellström T., Garvey J. S. Characterization studies on the cadmium-binding proteins from two species of New Zealand oysters. Environ Health Perspect. 1986 Mar;65:57–62. doi: 10.1289/ehp.866557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Pulido P., Kägi J. H., Vallee B. L. Isolation and some properties of human metallothionein. Biochemistry. 1966 May;5(5):1768–1777. doi: 10.1021/bi00869a046. [DOI] [PubMed] [Google Scholar]
  9. Ridlington J. W., Fowler B. A. Isolation and partial characterization of a cadmium-binding protein from the American oyster (Crassostrea virginica). Chem Biol Interact. 1979 May;25(2-3):127–138. doi: 10.1016/0009-2797(79)90041-3. [DOI] [PubMed] [Google Scholar]
  10. Rupp H., Weser U. Circular dichroism of metallothioneins. A structural approach. Biochim Biophys Acta. 1978 Mar 28;533(1):209–226. doi: 10.1016/0005-2795(78)90565-2. [DOI] [PubMed] [Google Scholar]
  11. Stone H. C., Wilson S. B., Overnell J. Cadmium-binding proteins in the scallop Pecten maximus. Environ Health Perspect. 1986 Mar;65:189–191. doi: 10.1289/ehp.8665189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Weser U., Rupp H., Donay F., Linnemann F., Voelter W., Voetsch W., Jung G. Characterization of Cd, Zn-thionein (metallothionein) isolated from rat and chicken liver. Eur J Biochem. 1973 Nov 1;39(1):127–140. doi: 10.1111/j.1432-1033.1973.tb03111.x. [DOI] [PubMed] [Google Scholar]

Articles from Environmental Health Perspectives are provided here courtesy of National Institute of Environmental Health Sciences

RESOURCES