Cadmium-binding proteins in the scallop Pecten maximus. | Zendy

Howard C. Stone | Zendy; S. Brian Wilson | Zendy; J. Overnell | Zendy

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Cadmium-binding proteins in the scallop Pecten maximus.

Author(s) -

Howard C. Stone,

S. Brian Wilson,

J. Overnell

Publication year - 1986

Publication title -

environmental health perspectives

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.257

H-Index - 282

eISSN - 1552-9924

pISSN - 0091-6765

DOI - 10.1289/ehp.8665189

Subject(s) - metallothionein , cadmium , pecten maximus , sephadex , scallop , fraction (chemistry) , dry weight , chemistry , biochemistry , biology , chromatography , mollusca , zoology , bivalvia , botany , enzyme , ecology , organic chemistry

Scallops, Pecten maximus, accumulate cadmium naturally in the digestive gland to a level of approximately 100 ppm wet weight. Of this cadmium, 60% was soluble and was composed of three weight classes as judged by Sephadex G-100 chromatography. Of the soluble cadmium, 60% was in the 55,000 molecular weight range and 20% each in an excluded fraction and a 10,000 molecular weight fraction. The 55,000 molecular weight fraction, after further purification, showed a maximum cadmium concentration of 1.4% by weight. The cadmium was thiolate bound but not as strongly bound as in the case of metallothionein. The 10,000 molecular weight fraction was a metallothionein-like protein.

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