EFFECT OF SALTS ON THE INTERACTION OF OXIDIZED GLUTATHIONE WITH DIBASIC AMINO-ACIDS

The interaction of oxidized glutathione (GSSG) with dibasic amino acid s was studied with charge-transfer chromatography carried out on unimp regnated cellulose layers in the absence and presence of LiCl, NaCl, K Cl, MgCl, and CaCl2. GSSG decreased in each case the apparent lipophil icity of dibasic amino acids, indicating some type of interaction. Cal culations proved that the strength of GSSG - dibasic amino acid intera ction decreases with increasing concentration of salts suggesting a hy drophilic character of interaction. It can be assumed that electrostat ic forces between the carboxyl group of GSSG and the amino groups of a mino acids are involved in the interaction. GSSG binds stronger to arg inine than to lysine and ornithine suggesting that arginine is probabl y the primary binding site in proteins for GSSG.