The oligomeric structure of rat liver microsomal glutathione transferase studied by chemical cross-linking.
The oligomeric structure of rat liver microsomal glutathione transferase was investigated using four different chemical cross-linking reagents. Studies were performed with the isolated enzyme, with the enzyme incorporated into phosphatidyl choline liposomes and with rat liver microsomes. Cross-linking was analyzed by use of SDS-PAGE combined with Western blotting. Our results strongly suggest that the microsomal glutathione transferase is a trimer in situ in the endoplasmic reticulum, as well as in the purified state and in proteoliposomes. These results lend strong support to previous studies, involving hydrodynamic characterization and radiation inactivation, indicating that the microsomal glutathione transferase is a trimeric enzyme.
Lundqvist
G
G
Department of Toxicology, Karolinska Institutet, Stockholm, Sweden.
Yücel-Lindberg
T
T
Morgenstern
R
R
D000818:Animals; D003432:Cross-Linking Reagents; D005982:Glutathione Transferase / Q000737:chemistry*; D046911:Macromolecular Substances; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D011487:Protein Conformation; D051381:Rats; D017207:Rats, Sprague-Dawley
D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D005982:Glutathione Transferase