Isolation and characterization of a hepatic metallothionein from mice.
Mice were given cadmium chloride orally for 18 weeks, after which they were given two subcutaneous injections of cadmium chloride. Cadmium-and zinc-containing proteins were obtained from livers by ultracentrifugation, Sephadex chromatography and isoelectric focusing. Metallothionein with apI of 4.2 at 8 degrees C was separated from other proteins (possibly including other forms of metallothionein) by the isoelectric procedure. The metallothionein with pI = 4.2 had a high E250, reflecting abundant Cd-SH bonds, in accord with amino acid analysis, which gave a cysteine content of 34.6 residues % and showed an absence of aromatic amino acids. These results indicated a very high purity of the form of metallothionein isolated after isoelectric focusing.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002104:Cadmium / Q000032:analysis; D002850:Chromatography, Gel; D003545:Cysteine / Q000032:analysis; D007525:Isoelectric Focusing; D008099:Liver / Q000032:analysis*; D008297:Male; D008667:Metalloproteins; D008668:Metallothionein / Q000032:analysis / Q000302:isolation & purification; D051379:Mice; D008808:Mice, Inbred CBA; D014461:Ultracentrifugation; D015032:Zinc / Q000032:analysis
D000596:Amino Acids; D008667:Metalloproteins; D002104:Cadmium; D008668:Metallothionein; D015032:Zinc; D003545:Cysteine