Increase of low-molecular weight polypeptides of rat liver mitochondrial membrane by 2-mercaptopropionylglycine.

Having used 2-mercaptopropionylglycine in successful treatment of chronic hepatitis the mode of action of the reagent was further studied in rat liver mitochondrial membrane. Gradient polyacrylamide gel electrophoresis was employed for this purpose. It was found that after incubation of the mitochondria with ADP and 2-mercaptopropionylglycine and isolation of mitochondrial membranes the amount of low-molecular weight polypeptides was significantly increased. These polypeptides belong to the molecular weight ranges of the epsilon-subunits of the mitochondrial ATPase and of the oligomycin binding site. A working hypothesis is formed that the drug may improve anchoring the ATPase molecule at the membrane site. Such mechanism may elucidate previous biochemical findings, and, in particular, underlines the structure-preserving effect of 2-mercaptopropionylglycine in mitochondria.