Dogfish metallothionein--II. Electrophoretic studies and comparison with rat metallothionein.
A low-molecular weight metal-binding protein has been isolated and characterized as metallothionein in the liver of the dogfish (Scyliorhinus canicula). This protein is present in both male and female animals and both control and cadmium-treated (both water and i.p. administration) animals as revealed by SDS-PAGE studies. Dogfish metallothionein shows the same metal-dependent anomalous behaviour as rat metallothionein in SDS-PAGE. SDS-PAGE is a good method to identify a protein as metallothionein.
Hidalgo
J
J
Flos
R
R
D000818:Animals; D001797:Blood Protein Electrophoresis; D002104:Cadmium / Q000494:pharmacology; D004284:Dogfish / Q000378:metabolism*; D005260:Female; D066298:In Vitro Techniques; D008099:Liver / Q000032:analysis*; D008297:Male; D008668:Metallothionein / Q000032:analysis*; D051381:Rats; D012737:Sex Factors; D012754:Sharks / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate
D002104:Cadmium; D012967:Sodium Dodecyl Sulfate; D008668:Metallothionein