Separation and purification of (Cd, Cu, Zn)-metallothionein in carp hepato-pancreas.
1. Cd-binding protein was isolated from the hepato-pancreas of carp administered CdCl2 (2 mg/kg). 2. This protein had a high absorption at 254 nm derived from Cd-mercaptide binding, and a low absorption at 280 nm derived from the absence of aromatic amino acids; the authors recognized the presence of two types. 3. The amino acid composition of the proteins was determined. The contents of cysteine residues were 34.24% and 31.90% in MT-I and -II respectively. Tyrosine, phenylalanine, tryptophan, histidine, leucine and arginine residues were absent in both types.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002347:Carps / Q000378:metabolism*; D003300:Copper / Q000302:isolation & purification; D003530:Cyprinidae / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D008099:Liver / Q000032:analysis*; D008667:Metalloproteins / Q000302:isolation & purification*; D008668:Metallothionein / Q000302:isolation & purification*; D008970:Molecular Weight; D010179:Pancreas / Q000032:analysis*; D015032:Zinc / Q000302:isolation & purification
D000596:Amino Acids; D008667:Metalloproteins; C004203:cadmium-binding protein; D003300:Copper; D008668:Metallothionein; D015032:Zinc