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Metabolism and toxicity of trace metals by the mussel, Mytilus edulis. Final report

Technical Report ·
OSTI ID:5002148
Mercury-induced, low molecular weight, metal-binding proteins were isolated from the marine mussel, Mytilus edulis, and used as antigen in the development of an enzyme-linked immunosorbent assay (ELISA) for quantitation of the proteins. Partial characterization of the isolated protein indicated close similarities with metallothionein, in that it was cysteine-rich and lacked aromatic amino acids. Glycine was also present at high levels. The molecular weight, however, was twice that expected for metallothionein, and it appears that the predominant metal-binding protein in this molluscan species exists as a dimer. Polyclonal antibodies against this protein were previously produced in goats and purified to an IgG fraction by ammonium sulfate precipitation and DEAE ion exchange chromatography. Ouchterlony analysis and ELISA showed that these antibodies were cross-reactive with two other charge variants of mercury-induced metal-binding proteins of M. edulis, but not with rabbit metallothionein. The ELISA was based on an indirect, competitive procedure utilizing a rabbit anti-goat IgG-horseradish peroxidase conjugate as the second antibody. The routine working range of the ELISA was between 1 and 21 ng antigen. Application of this assay to cytosolic extracts of mussel gills indicated 0.5 ug/g wet tissue weight in gills of control mussels and elevated levels up to 1780 ug/g following exposure to mercury, cadmium, or copper for 28 days. 15 refs.
Research Organization:
Pennsylvania State Univ., University Park (USA). Dept. of Biology
DOE Contract Number:
FG02-86ER60410
OSTI ID:
5002148
Report Number(s):
DOE/ER/60410-1; ON: DE87001761
Country of Publication:
United States
Language:
English