DENATURATION OF HEMOGLOBIN IN THE PRESENCE OF TANNIC ACID

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/2014.48.1.023

Keywords:

human hemoglobin, tannic acid, denaturation, fluorescence spectroscopy, 3D spectra, UV/vis spectroscopy

Abstract

hermal denaturing of human hemoglobin (HHb) in the presence of tannic acid (TA) was studied by fluorescence and UV/vis spectroscopy in 30–66°C temperature range. To study more detailed structural changes in HHb molecule caused by temperature rise in the presence of TA, the excitation/emission fluorescence (3D spectra) matrix method has been used. It has been shown, that the increase of temperature causes more pronounced structural changes in the flexible areas of protein containing aromatic amino acids than in the rigid α, β polypeptide chains. It was revealed that the presence of TA causes structural changes in HHb.

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Published

2014-03-17

How to Cite

Grigoryan, K.R., and L.S. Sargsyan. 2014. “DENATURATION OF HEMOGLOBIN IN THE PRESENCE OF TANNIC ACID”. Proceedings of the YSU B: Chemical and Biological Sciences 48 (1 (233):23-27. https://doi.org/10.46991/PYSU:B/2014.48.1.023.

Issue

Vol. 48 No. 1 (233) (2014)

Section

Chemistry

License

Copyright (c) 2014 Proceedings of the YSU

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

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