INFLUENCE OF DIMETHYLSULFOXIDE ON UREA-BOVINE SERUM ALBUMIN INTERACTIONS

Authors

  • K.R. Grigoryan Chair of Physical and Colloids Chemistry, YSU, Armenia
  • L.S. Sargsyan Chair of Physical and Colloids Chemistry, YSU, Armenia

DOI:

https://doi.org/10.46991/PYSU:B/2012.46.2.008

Keywords:

dimethylsulfoxide, urea bovine serum albumin, thermal and chemical denaturation, reversible multistep mechanism

Abstract

Using classical physicochemical (calorimetry, electroconductivity, pH-metry) and spectroscopic (IR, UV/vis) methods the effect of dimethylsulfoxide (DMSO) on urea bovine serum albumin (BSA) interactions have been studied. First of all the structural peculiarities of urea aqueous solutions in the presence of DMSO and then in these solutions the thermal and chemical denaturation of BSA has been determined. It has been established that in DMSO containing solutions (up to 10%, v/v) urea solvate shell structure changes by inclusion of DMSO molecules. At mentioned conditions BSA thermal and chemical denaturation proceeds according to reversible multistep mechanism. After denaturation some structural unities of BSA ternary structure remain.

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Published

2012-05-10

How to Cite

Grigoryan, K.R., and L.S. Sargsyan. 2012. “INFLUENCE OF DIMETHYLSULFOXIDE ON UREA-BOVINE SERUM ALBUMIN INTERACTIONS”. Proceedings of the YSU B: Chemical and Biological Sciences 46 (2 (228):8-13. https://doi.org/10.46991/PYSU:B/2012.46.2.008.

Issue

Vol. 46 No. 2 (228) (2012)

Section

Chemistry

License

Copyright (c) 2012 Proceedings of the YSU

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

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