title: Dogfish metallothionein--I. Purification and characterization and comparison with rat metallothionein.
abstract: A low-molecular weight metal-binding protein has been found in the liver of the dogfish (Scyliorhinus canicula) in both control and cadmium-treated animals and in both male and female animals. This protein is present as Zn, Cu-protein in control and as Cd, Zn, Cu-protein cadmium-treated (both water and i.p. administration) animals. This hepatic protein was characterized as metallothionein from several properties related to mammalian metallothionein. A different response to cadmium administration between sexes is suggested.
authors.forename: J
authors.initials: J
authors.lastname: Hidalgo
authors.forename: R
authors.initials: R
authors.lastname: Flos
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002104:Cadmium / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D004284:Dogfish / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D066298:In Vitro Techniques; D008099:Liver / Q000032:analysis*; D008297:Male; D008668:Metallothionein / Q000032:analysis / Q000302:isolation & purification*; D051381:Rats; D011919:Rats, Inbred Strains; D012754:Sharks / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate
chemical_list: D000596:Amino Acids; D002104:Cadmium; D012967:Sodium Dodecyl Sulfate; D008668:Metallothionein