Isolation and partial characterization of a cadmium-binding protein from the American oyster (Crassostrea virginica).
American oysters (Crassostrea virginica) were exposed to 0.1 ppm cadmium for 0--15 days in a flowing seawater system and then placed into clean flowing seawater for 24 h prior to sacrifice. Whole oysters were homogenized and a cadmium-binding protein isolated and purified by a process of centrifugation, heat-treatment, Sephadex G-75 chromatography, DEAE cellulose chromatography and disc gel electrophoresis. A highly anionic protein which is not present in control oysters was found to be present in cadmium-exposed animals after 3 days of treatment and to increase in concentration at succeeding time points. The protein does not extensively bind zinc or copper. Amino acid analysis of the purified protein disclosed an amino acid composition characterized by a high percentage of dicarboxylic amino acids and relatively little cysteine.
D000818:Animals; D002104:Cadmium; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003300:Copper; D004591:Electrophoresis, Polyacrylamide Gel; D008667:Metalloproteins / Q000302:isolation & purification*; D008668:Metallothionein; D010125:Ostreidae / Q000032:analysis*; D015032:Zinc
D008667:Metalloproteins; C004203:cadmium-binding protein; D002104:Cadmium; D003300:Copper; D008668:Metallothionein; D015032:Zinc