INFLUENCE OF DIMETHYLSULFOXIDE ON THE FLUORESCENCE BEHAVIOR OF HUMAN SERUM ALBUMIN STUDIED BY EXCITATIONEMISSION MATRIX FLUORESCENCE SPECTROSCOPY METHOD

Authors

  • K.R. Grigoryan Chair of Physical and Colloids Chemistry, YSU, Armenia
  • H.A. Shilajyan Chair of Physical and Colloids Chemistry, YSU, Armenia

DOI:

https://doi.org/10.46991/PYSU:B/2013.47.1.050

Keywords:

human serum albumin, excitation-emission matri, fluorescence spectroscopy, dimethylsulfoxide, structural changes

Abstract

Three-D excitation-emission matrix (EEM) fluorescence spectra of Human Serum Albumin (HSA) were measured at the presence of dimethylsulfoxide (DMSO) at t=25°C during 270 min before and after adding DMSO in different concentrations. It has been shown that DMSO at low concentrations (5%) increase heat-resistance of HSA changing the solvent structure around the protein molecule, it causes conformational changes as well in protein. Drastic changes are observed in the protein struture at DMSO higher concentration (20%). Keywords: human serum albumin, excitation-emission matrix, fluorescence spectroscopy, dimethylsulfoxide, structural changes.

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Published

2013-03-10

How to Cite

Grigoryan, K.R., and H.A. Shilajyan. 2013. “INFLUENCE OF DIMETHYLSULFOXIDE ON THE FLUORESCENCE BEHAVIOR OF HUMAN SERUM ALBUMIN STUDIED BY EXCITATIONEMISSION MATRIX FLUORESCENCE SPECTROSCOPY METHOD”. Proceedings of the YSU B: Chemical and Biological Sciences 47 (1 (230):50-53. https://doi.org/10.46991/PYSU:B/2013.47.1.050.

Issue

Vol. 47 No. 1 (230) (2013)

Section

Short Communications

License

Copyright (c) 2013 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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