[Study of the conditions for the breakdown of mixed disulfides between aminothiol protectors and cell proteins as factors that determine the stability of the disulfide bonds].

A glutathione reductase activity was unaltered in thymus and liver tissue and slightly increased in spleen of rats within 15-30 min after administration of a radioprotector mercaptoethylamine. At the same time an activation of unspecific disulphide reductase occured. The both enzymes participated in spliting of mercaptoethylamine disulphides coupled with proteins. The radioprotective effectiveness of the aminothiol was, though partially, due to development of these disulfides. Retention of disulfides between the protector and cell proteins could be extended up to 1 h. by administration of mercaptoethylamine into rats with decreased content of endogenous glutathione, caused by the previous treatment with cyclohexene.