Abstract
A zinc-binding protein was purified to homogeneity from a scallop, Patinopecten yessoensis. The protein was synthesized under zincenriched conditions like metallothioneins (MTs). The protein, however, did not satisfy the criteria for classification as MTs in amino acid composition because the cysteine content was extremely low and asparatic and glutamic acids were the predominant residues. These results suggested that the Zn-binding protein purified in this study was a new inducible protein and involved in zinc storage in the scallop.
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