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Thiolation and Disulphide Cross-Linking of Insulin to Form Macromolecules of Potential Therapeutic Value

  • M. Mahbouba
  • H. J. Smith
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)

Abstract

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 macromolecules and was probably bound within an insulin-modified insulin hexamer through coordination to copper.

Keywords

Disulphide Bond Potassium Ferricyanide Disc Electrophoresis Cupric Chloride Native Insulin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • M. Mahbouba
    • 1
  • H. J. Smith
    • 1
  1. 1.Welsh School of PharmacyUniversity of Wales Institute of Science and TechnologyCardiff S. Wales, UK

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