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Theoretical and Experimental Chemistry

, Volume 26, Issue 1, pp 98–101 | Cite as

Solvation effects in human serum albumin radiolysis in the presence of dimethyl sulfoxide

  • V. K. Pogorelyi
  • V. N. Barvinchenko
  • V. V. Turov
Brief Communications
  • 41 Downloads

Abstract

PMR and electrophoresis have been applied to examine hydration changes in protein molecules due to the presence of the electron donor dimethylsulfoxide DMSO, which influences the radiolysis of human serum albumin HSA. The reactions of aqueous HSA with added DMSO show that the DMSO on the one hand acts as a protector, which prevents the formation of low-molecular protein forms on reaction with hydroxyl radicals, and on the other alters the protein hydration, which facilitates thiol-di-sulfide exchange, which leads to oligomers.

Keywords

Hydration Albumin Hydroxyl DMSO Electrophoresis 
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 Publishing Corporation 1990

Authors and Affiliations

  • V. K. Pogorelyi
    • 1
  • V. N. Barvinchenko
    • 1
  • V. V. Turov
    • 1
  1. 1.Pisarzhevskii Physical Chemistry InstituteUkrainian Academy of SciencesKiev

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