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Computational Molecular Biology 2015, Vol. 5, No. 1, 1-13
http://cmb.biopublisher.ca
7
Abbreviation: aa: amino acids; MW: molecular weight; p
I
: isoelectric point; AI: aliphatic index; HBA: α-chain of hemoglobin
HBB
:
ß-chain of hemoglobin;
C. d
:
Camelus
dromedarius
;
C. b
:
Camelus
bactrainus
;
C. d
:
Camelus
ferrus
;
B. t
:
Bos
taurus
;
E. c
:
Equus cabalus
;
H. s
:
Homo
sapiens
.
Charged AAs (amino acids) for HBA and HBB in
Camelus
family are more than human (Table 2). It
could also be possible that the redox state of camel
blood or the internal environment of erythrocytes as
variations of blood pH may contribute to the
reduction of HbA1c levels, as the reseach of Bazzi et
al., 2013. As well as Lin et al., 1976 are stated
Camelus dromedarius
hemoglobin possesses more
positive charges on paper electrophoresis than does
human HBA, and showed that been consist of only a
single component (Lin et al., 1976). Some
researchers are declared that erythrocytes of camels
is more resistant to hemolysis in comparison with
cattle, sheep, goats, pigs, mice, man and other
animals (Al-Qarawi et al., 2004; Oyewale et al.,
2011). As hemoglobin from
Camelus dromedarius
provides an interesting case of adaptation to life
condition in deserts at extremely high temperatures
(Balasubramanian et al., 2009) The proportion of
water in the camel erythrocytes that is osmotically
non-removable is almost three times greater than in
human, which seems leading to extremely good
resistance of camel erythrocytes to osmotic change
(Bognera et al., 2005). As influence of food on
glycosylation of hemoglobin (GHB) in the birds is
demonstrated (Miksik and Hodny, 1992).
2.4 Homology measurement
Based on information demonstrated in Table 3,
similarity of HBA and HBB between
Camelus
bactrianus
and Camelus dromedarius was 100%, as
100% query coverage (Table 3). However, the
similarity for ß-chain of HB (HBB) was 100% and
100% query coverage in species of
Camelus
family.
The both alpha and beta chains of Hb were 84%
similarity with 100% query coverage between
Camelus
family and
Homo sapiens
. The similarity
between α-chain of Hb
Camelus
family versus
Bos
taurus
and
Equus caballus
were 85% and 86%
respectively. Also resemblance of ß-chain of
Camelus
family versus
Bos taurus
and
Equus
caballus
were 83% and 82% respectively (Table 3).
Therefore alpha and beta chains of hemoglobin are
conserved in considered species. So it seems that,
depends on common function of hemoglobin in
order transferring oxygen by ferrous.
Table 3 Genome homology of α-chain (HBA) and ß-chain (HBB) of hemoglobin between mentioned species. The criterion of
identity as homology with E-value and query coverage is shown for each comparison between species
Hemoglobin chain Sequence
Indent
E-value
Query coverage
Camelus bactrianus
Vs.
dromedarius
(HBA)
100%
7e-103
100%
Camelus bactrianus
and
dromedarius
Vs.
ferus
(HBA)
100%
6e-102
98%
Camelus bactrianus
and
dromedarius
Vs.
Bos taurus
(HBA)
85%
3e-87
100%
Camelus bactrianus
and
dromedarius
Vs.
Equus caballus
(HBA)
86%
2e-88
100%
Camelus bactrianus
and
dromedarius
Vs.
Homo sapiens
(HBA)
84%
4e-88
100%
Camelus bactrianus
Vs.
dromedarius
(HBB)
100%
5e-110
100%
Camelus bactrianus
and
dromedarius
Vs.
ferus
(HBB)
100%
5e-110
100%
Camelus bactrianus, dromedarius
and
ferus
Vs.
Bos taurus
(HBB)
83%
9e-82
97%
Camelus bactrianus, dromedarius
and
ferus
Vs.
Equus caballus
(HBB)
82%
4e-82
100%
Camelus bactrianus, dromedarius
and
ferus
Vs.
Homo sapiens
(HBB)
84%
1e-92
100%
Camelus ferus
(HBA) Vs.
Camelus bactrianus
and
dromedarius
(HBB)
39%
3e-25
97%
Camelus ferus
(HBB) Vs.
Camelus bactrianus
and
dromedarius
(HBA)
39%
9e-30
97%
Camelus ferus
(HBA) Vs.
Camelus ferus
(HBB)
39%
3e-25
97%
Abbreviations: HBA: α-chain of hemoglobin; HBB: ß-chain of hemoglobin; Vs: versus