Role of Purinergic Receptors of Erythrocytes in the Regulation of Conformation and Oxygen- and NO-Transporting Capacity of Hemoglobin

Raman spectroscopy was used to investigate changes in hemoglobin conformation and its ability to transfer O 2 and NO induced by activation of purinergic receptors of erythrocytes with extracellular ATP. It was found that addition of ATP in a final concentration of 0.1 mM and higher to erythrocyte su...

Full description

Saved in:
Bibliographic Details
Published in:Bulletin of experimental biology and medicine 2015-06, Vol.159 (2), p.213-216
Main Authors: Kovalenko, S. S., Yusipovich, A. I., Parshina, E. Yu, Maksimov, G. V.
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - pharmacology
Biomedical and Life Sciences
Biomedicine
Biophysics and Biochemistry
Cell Biology
Dose-Response Relationship, Drug
Erythrocytes - metabolism
Glycosylated hemoglobin
Hematoporphyrins - chemistry
Hemoglobins - chemistry
Hemoglobins - metabolism
Humans
Internal Medicine
Laboratory Medicine
Nitric Oxide - metabolism
Oxygen - metabolism
Oxyhemoglobin
Pathology
Protein Conformation
Raman spectroscopy
Receptors, Purinergic - metabolism
Spectrum Analysis, Raman
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Raman spectroscopy was used to investigate changes in hemoglobin conformation and its ability to transfer O 2 and NO induced by activation of purinergic receptors of erythrocytes with extracellular ATP. It was found that addition of ATP in a final concentration of 0.1 mM and higher to erythrocyte suspension was followed by changes in hematoporphyrin conformation, while addition of ATP in a concentration of 1 mM and higher increased the proportion of oxyhemoglobin and NO-associated hemoglobin complexes. In case of purinergic receptors activation in blood erythrocytes, significant changes in hemoglobin conformation were observed only at a final ATP concentration of 5 mM, probably due to buffer properties of the blood.
ISSN:0007-4888
1573-8221
DOI:10.1007/s10517-015-2925-6