Isolation and characterization of a metallothionein-like protein from monkey brain. Toxicology 1987 Jul;45(1):53-64
Date
07/01/1987Pubmed ID
3603575DOI
10.1016/0300-483x(87)90114-4Scopus ID
2-s2.0-0023227114 (requires institutional sign-in at Scopus site) 20 CitationsAbstract
A cadmium-binding protein from monkey brain has been isolated, purified and characterized. The absorption spectrum of this protein indicates the presence of Cu-Zn thionein in the normal monkey brain which has a strong affinity to bind cadmium. On cadmium exposure the protein sequestered most of the cadmium which entered the brain. The apparent molecular weight of this protein as determined on a gel filtration column calibrated with marker proteins has been found to be in the range of 11,500-12,000 Da. The ratio of absorbance at 254 nm/280 nm is more than 1 indicating the presence of cadmium-mercaptide bonds, which was further confirmed by the presence of 15 cysteine residues. Polyacrylamide gel electrophoresis of the protein shows 3 bands indicating the presence of 3 isometallothionein forms. Unlike hepatic or renal thioneins, the cadmium-binding protein in brain is not inducible following administration of cadmium. However, when antibodies raised against hepatic metallothionein were cross-reacted with brain Cd-binding protein, a line of identity was observed, indicating the 2 proteins are immunologically identical and share a high degree of structural similarity.
Author List
Gulati S, Paliwal VK, Sharma M, Gill KD, Nath RAuthor
Vipin Paliwal PhD Associate Professor in the Physics & Chemistry department at Milwaukee School of EngineeringMESH terms used to index this publication - Major topics in bold
AnimalsBrain
Brain Chemistry
Cadmium
Cadmium Chloride
Chromatography, Gel
Copper
Macaca mulatta
Male
Metallothionein
Zinc
