Abstract
1. 1. In Allolobophora caliginosa , a Cd-binding protein distinct in charge from Cd-BP 14, a Cd-binding protein previously isolated from the same oligochaete species [Nejmeddine et al. (1992) Comp. Biochem. Physiol. 101C, 601–605], has been purified by a three-step chromatographic procedure including gel permeation and cation-exchange chromatography. 2. 2. This Cd-binding protein exists in a monomeric form with a molecular weight of 14 kDa and does not contain carbohydrate. 3. 3. The purified protein significantly absorbed at 280 nm and its amino acid composition revealed the presence of a high level of aromatic amino acids and a lack of cysteine, indicating that the molecule is distinct from metallothioneins. 4. 4. By contrast, except for its chromatographic behavior on an ion-exchange chromatography column, the metalloprotein was found to be similar to Cd-BP 14. We thus conclude that it represents a charge-variant of Cd-BP 14.
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