Reconstruction of intact gamma-globulin from S-sulfonated gamma-globulin in vivo.
The conversion of the S-surfonate group in a peptide to a disulfide bond has been observed in vitro. This paper reports that the conversion of this group in human S-sulfonated gamma-globulin (S-GG) appeared to occur in vivo judging from the change in molecular weight of S-GG observed in the presence of sodium dodecyl sulfate (SDS) and the restoration of hemolytic activity.
D000818:Animals; D001665:Binding Sites; D004220:Disulfides / Q000032:analysis; D004589:Electrophoresis, Disc; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D046911:Macromolecular Substances; D011485:Protein Binding; D011817:Rabbits; D012967:Sodium Dodecyl Sulfate; D013451:Sulfonic Acids; D014118:Toxins, Biological / Q000494:pharmacology; D005719:gamma-Globulins / Q000096:biosynthesis / Q000494:pharmacology
D004220:Disulfides; D046911:Macromolecular Substances; D013451:Sulfonic Acids; D014118:Toxins, Biological; D005719:gamma-Globulins; D012967:Sodium Dodecyl Sulfate