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Computational Molecular Biology 2015, Vol. 5, No. 1, 1-13
http://cmb.biopublisher.ca
1
Research Article Open Access
In
Silico
investigation for hemoglobin characterizations leads to new aspects
in susceptibility to glycosylation
Reza Talebi
1
, Ahmad Ahmadi
1
, Fazlolah Afraz
2
, Seyed Zeyaedin Mirhoseini
3
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
Corresponding author email
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
© 2015
Talebi et al., 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
Abstract
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; p
I
, Isoelectric Point.
Keywords
In silico
; Multiple alignments; Hemoglobin; Glycosylation; HbA1c.
Introduction
Globins are unique molecules that could transport
oxygen through body tissues. Hemoglobin and
myoglobin are two kinds of globins that are
respectively responsible in blood and muscle. They
are found in all vertebrates and some kinds of
invertebrates. Hemoglobin structure in vertebrates
shows the typical globin fold accommodating a heme
group which reversibly binds oxygen to its central
ferrous atom compound. Adult hemoglobin is a
[α(2):β(2)] tetrameric hemoprotein with molecular
mass of each chain is 15 kDa which is found in
erythrocytes, where it is responsible for binding
oxygen in the lung and transporting the bound oxygen
throughout the body where it is used in aerobic
metabolic pathways (Dickerson and Geiss, 1983; Paoli
and Nagai, 2004; Pairet and Jaenicke, 2010) The
shapes of erythrocytes in the mammalian(s) except of
camelidae family are spherical and concave, but in the
camelidae, are oval form and nucleus less
(Goniakowska-Witalinska and Witalinski, 1976;
Azwai et al., 2007). The erythrocytes of camelidae are
highly resistant against osmotic hemolysis, so are able
to expand up to 240% of their original volume without
rupturing in hypotonic solutions (Oyewale et al., 2011).
Glycosylated hemoglobin (GHB) or Maillard reaction
is formed by a non-enzymatic interaction between
glucose and N-terminal valine and lysine residue of
the β-chain of HB, maybe should be causes rise to
HbA1c- a type of HB commonly associated with
diabetes (Rohlfing et al., 2002; Wautier and Schmidt,
2004; Soranzo, 2011). As HbA1c is resided for long
term and has’nt decomposed, HbA1c concentrations
have been used for decades to assess the effects of
long-term glycemic control in diabetic patients.10