• 1 January 1976
    • journal article
    • research article
    • Vol. 4  (6) , 513-516
Abstract
The covalent binding of 3H-methyldopa to microsomal protein in the presence of NADPH and O2 was studied in various microsomal preparations. Rat and mouse liver microsomes showed high binding, and hamster and guinea pig liver microsomes gave intermediate values, no binding was seen with rabbit liver microsomes. No activation of methyldopa was detected with kidney microsomes. Lung microsomes from rats, guinea pigs and rabbits were active with respect to methyldopa binding and the reactions were totally blocked by superoxide dismutase. There was no sex difference in the binding of methyldopa in liver microsomes from adult rats. No methyldopa activation could be detected in fetal liver microsomes; a rapid increase in activity to above adult levels occurred during the first 2 days after birth.