In Silico investigation for hemoglobin characterizations leads to new aspects in susceptibility to glycosylation  

Reza Talebi1 , Ahmad Ahmadi1 , Fazlolah Afraz2 , Seyed Zeyaedin Mirhoseini3
1. Department of Animal Genetics, Faculty of Agriculture, Bu-Ali Sina University, Hamedan, Iran
2. Department of Animal Genetics, Agricultural Biotechnology Research Institute of Iran, Rasht, Iran
3. Department of Animal Genetics, Faculty of Agriculture, University of Guilan, Rasht, Iran
Author    Correspondence author
Computational Molecular Biology, 2015, Vol. 5, No. 1   doi: 10.5376/cmb.2015.05.0001
Received: 10 Dec., 2014    Accepted: 25 Dec., 2014    Published: 29 Dec., 2014
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This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Talebi et al., 2015, In Silico investigation for hemoglobin characterizations leads to new aspects in susceptibility to glycosylation, Computational Molecular Biology, Vol.5, No.1, 1-13 (doi: 10.5376/cmb.2015.05.0001)


In silico analysis were performed between some species for hemoglobin characterizations specially resistivity to glycosylation. Multiple alignments of both hemoglobin subunits were revealed L-K-V-K-E-G-E-A-L-R-P-T-F-F-D-L-S-A-V- K-H-G-K-V-H-D-L-S-L-H-K-L-V-D-P-N-F-L-L-L-A-F-T-P-A-K-V-L-Y conserved in camel, human, cow and horse entirely. Hemoglobin sequences are well conserved in evolution and between species. Camelus families HBA were in same cluster (91% bootstrapping). However for HBB they were in same cluster (95% bootstrapping). Camel hemoglobin appeared to be more basic than either that of other species. Based on isoelectric points, camel HBB has high mobility than HBA in electrophoresis. The charged and hydrophilic amino acids of hemoglobin in camel were more than human. The non-enzymatic binding of glucose to the protein or HbA1c is revealed both subunits hemoglobin in human is resistance to N-glycosylation but camel HBB is only resistant to O-glycosylation. HBB is less susceptible to glycosylation than HBA. Also HBB has critical roles in camel for instance resistivity to glycosylation and diabetes subsequently.

Abbreviations: HB, Hemoglobin; HBA, α-chain of hemoglobin; HBB, β-chain of hemoglobin; GHB, glycosylated hemoglobin; AA, Amino Acid; NA, nucleic acid; Vs., versus; pI, Isoelectric Point.

In silico; Multiple alignments; Hemoglobin; Glycosylation; HbA1c.
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