Thiolation and disulphide cross-linking of insulin to form macromolecules of potential therapeutic value.
Macromolecules have been prepared containing native insulin carried by a modified insulin skeleton made by partially thiolating the insulin hexamer and forming intermolecular cross-links through disulphide bridges. Oxidation of partially thiolated insulin (0.5-0.7 SH group/mole), formed by reacting insulin with AHTL, with, (a) potassium ferricyanide, (b) Cu++-oxygen gave water soluble macromolecules containing 20-26 and 410-708 monomer units respectively which had rod-random coil shape (light scattering). The larger molecules formed by (b) contained 8g-atom CU++/hexamer unit and insulin. The insulin was firmly bound within the marcomolecules and was probably bound within an insulin-modified insulin hexamer through coordination to copper.
D055598:Chemical Phenomena; D002621:Chemistry; D003300:Copper / Q000032:analysis; D004220:Disulfides; D006710:Homocysteine; D007328:Insulin / Q000627:therapeutic use; D007700:Kinetics; D007783:Lactones; D046911:Macromolecular Substances; D008722:Methods; D010084:Oxidation-Reduction; D010100:Oxygen; D011487:Protein Conformation; D013438:Sulfhydryl Compounds; D015032:Zinc / Q000032:analysis
D004220:Disulfides; D007328:Insulin; D007783:Lactones; D046911:Macromolecular Substances; D013438:Sulfhydryl Compounds; D006710:Homocysteine; D003300:Copper; D015032:Zinc; D010100:Oxygen