COMPARISON OF METHYL VIOLET INTERACTION WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY UV-DENATURATION METHOD

Authors

  • Mariam A. Shahinyan Chair of Biophysics, YSU, Armenia
  • Marieta S. Mikaelyan Chair of Biophysics, YSU, Armenia
  • Marine A. Parsadanyan Chair of Biophysics, YSU, Armenia
  • Ara P. Antonyan Chair of Biophysics, YSU, Armenia

DOI:

https://doi.org/10.46991/PYSU:B/2022.56.2.136

Keywords:

methyl violet, serum albumins, complex-formation, denaturation temperature, denaturation interval width

Abstract

In the present work the interaction of methyl violet (MV) with human serum albumin (HSA) and bovine serum albumin (BSA) has been studied by the UV-denaturation method and the obtained data were compared. The denaturation parameters – denaturation temperature and denaturation interval width, were determined. It was shown that MV, binding to serum albumins, stabilizes their structure. At the same time, the stabilization degree is different. It was also shown that BSA is stabilized more, than HSA, while binding to MV.

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Published

2022-08-28

How to Cite

Shahinyan, Mariam A., Marieta S. Mikaelyan, Marine A. Parsadanyan, and Ara P. Antonyan. 2022. “COMPARISON OF METHYL VIOLET INTERACTION WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY UV-DENATURATION METHOD”. Proceedings of the YSU B: Chemical and Biological Sciences 56 (2 (258):136-40. https://doi.org/10.46991/PYSU:B/2022.56.2.136.

Issue

Vol. 56 No. 2 (258) (2022)

Section

Biology

License

Copyright (c) 2022 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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