The presence of zinc-binding proteins in brain.
Zinc is one of the most abundant divalent metal ions in the brain, its concentration being greater than those of copper and manganese. Since free zinc ion is a potent inhibitor of sulfhydryl enzymes, we postulated that zinc in the brain most probably exists bound to macromolecules. As zinc-binding proteins in brain have not been characterized, we attempted to discover the occurrence and properties of these proteins. By using Sephadex G-75 column chromatography calibrated with proteins of known molecular weights, and by other techniques, we detected separate zinc-binding proteins, with apparent estimated molecular weights ranging from 15,000 to 210,000. Unlike the hepatic or renal zinc thioneins, the zinc-binding proteins in brain are not inducible following administration of zinc. Our interpretation of the results is that the major portion of the existing zinc in the brain is bound, and does not exist in free form.
D000818:Animals; D001921:Brain / Q000378:metabolism; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000032:analysis*; D002850:Chromatography, Gel; D008297:Male; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D013431:Sulfates / Q000378:metabolism; D014018:Tissue Distribution; D015032:Zinc / Q000378:metabolism; D019287:Zinc Sulfate
D002352:Carrier Proteins; D013431:Sulfates; C017800:zinc-binding protein; D019287:Zinc Sulfate; D015032:Zinc