Development of an intravenous gamma-globulin with Fc activities. II. Reconversion of S-sulfonated human gamma-globulin into the original gamma-globulin.
The reconversion of S-sulfonated antitetanus gamma-globulin (S-GG) into the original gamma-globulin was studied. S-sulfonate groups in S-GG could be converted into disulfide bonds in vitro. The conversion restored the greater part of both complement-fixing and skin-sensitizing activities. S-GG administered intravenously formed interchain disulfide bonds again in vivo, which was accompanied by restoration of the C-dependent passive hemolytic activity. Intravenous injection of S-GG did not cause a significant decrease in serum complement level.
D001711:Biotransformation; D003168:Complement Fixation Tests; D003165:Complement System Proteins / Q000032:analysis; D004220:Disulfides; D006801:Humans; D007141:Immunoglobulin Fc Fragments; D007275:Injections, Intravenous; D012882:Skin Tests; D013743:Tetanus Antitoxin; D005719:gamma-Globulins / Q000008:administration & dosage*
D004220:Disulfides; D007141:Immunoglobulin Fc Fragments; D013743:Tetanus Antitoxin; D005719:gamma-Globulins; D003165:Complement System Proteins