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Computational Molecular Biology 2015, Vol. 5, No. 1, 1-13
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6
than HBA in electrophoresis and resistance to
glycosylation subsequently. However we considered
isoelectric point in HBB for
Camelus
family were
more than human, cow and less than horse slightly
(Table. 2). In other word, ß-chain (HBB) in camel
and human has basic and neutral characteristics or
that it may influence glycosylation. It affects
mobility of protein during electrophoresis, so camel
and human HBB respectively have high and low
mobility during electrophoresis. As well as Bazzi et
al., 2013 declared camel Hemoglobin has higher
electrophoretic mobility than normal hemoglobin of
human or cow (Bazzi et al., 2013). The based on
Table 2, p
I
for α-chain of hemglobin (HBA) in
Camelus bactrianus
and
Camelus dromedarius
were
the same (9.39) more than
Camelus
ferus
(9.33)
slightly. Camel p
I
for both hemoglobin subunits were
more than Homo sapiens (Table 2). According to the
findings and Table 2, we noticed that a notable
difference in whole protein composition of HBA
between human and camel does not exist. So we
envision that other scenarios are affected to by
minimal glycosylation of camel hemoglobin - for
instance camel erythrocytes may restrict glucose
transport more than human-. Oyewale et al., 2011
were found that camel erythrocytes are more resistant
to hemolysis (or less osmotically fragile) than
donkey erythrocytes (Oyewale et al., 2011). In this
study, as illustrated in Figure 2, the
Camelus
family
hemoglobin has higher proportion of hydrophilic
amino acids (polar) compared with human (for
instance 20.42 and 21.28 for HBA between human
and camel respectively), and this gives the camel
hemoglobin its hydrophilic character
Table 2 Composition of hemoglobin. Predicted structural class of the whole protein: Alpha Deleage & Roux Modification of
Nishikawa & Ooi 1987
HBA
HBB
C. b
C. d
C. f
H. s
B. t
E. c
C. b
C. d
C. f
H.s
B.t
E.c
MW(kDa) 15.172 15.172 15.303 15.257 15.184 15.245 16.245
16.245 16.364 15.998 15.979
16.139
Length
141aa 141aa
142aa 142aa 142aa 142aa
147aa
147aa
148aa
147aa
145aa
147aa
p
I
9.39
9.39
9.33
9.12
8.87
9.12
8.71
8.71
9.05
7.11
6.64
6.77
A.I
87.234 87.234
86.62 90.775 93.521 93.451 94.762
94.762 94.517 93.469 92.759
95.442
Ala (A)
0.121
0.121
0.120 0.148 0.141 0.113
0.088
0.088
0.088
0.102
0.110
0.095
Cys (C)
0.007
0.007
0.007 0.007 0.000 0.007
0.007
0.007
0.007
0.014
0.007
0.007
Asp (D)
0.071
0.071
0.070 0.056 0.056 0.063
0.061
0.061
0.061
0.048
0.062
0.048
Glu (E)
0.021
0.021
0.021 0.028 0.035 0.021
0.048
0.048
0.047
0.054
0.055
0.068
Phe (F)
0.057
0.057
0.056 0.049 0.049 0.049
0.048
0.048
0.047
0.054
0.069
0.054
Gly (G)
0.064
0.064
0.063 0.049 0.063 0.070
0.088
0.088
0.088
0.088
0.069
0.095
His (H)
0.078
0.078
0.077 0.070 0.070 0.070
0.061
0.061
0.061
0.061
0.048
0.061
Ile (I)
0.007
0.007
0.007 0.000 0.000 0.000
0.000
0.000
0.000
0.000
0.000
0.000
Lys (K)
0.092
0.092
0.092 0.077 0.077 0.077
0.075
0.075
0.074
0.075
0.076
0.075
Leu (L)
0.128
0.128
0.127 0.127 0.141 0.148
0.129
0.129
0.128
0.122
0.117
0.129
Met (M)
0.007
0.007
0.014 0.021 0.014 0.014
0.014
0.014
0.014
0.014
0.021
0.014
Asn (N)
0.021
0.021
0.021 0.028 0.021 0.028
0.061
0.061
0.061
0.041
0.055
0.048
Pro (P)
0.043
0.043
0.042 0.049 0.042 0.042
0.027
0.027
0.027
0.048
0.028
0.034
Glu (Q)
0.007
0.007
0.007 0.007 0.007 0.007
0.014
0.014
0.014
0.020
0.021
0.027
Arg (R)
0.021
0.021
0.021 0.021 0.021 0.021
0.041
0.041
0.041
0.020
0.028
0.027
Ser (S)
0.085
0.085
0.085 0.077 0.092 0.092
0.048
0.048
0.047
0.034
0.041
0.041
Thr (T)
0.071
0.071
0.070 0.063 0.056 0.063
0.027
0.027
0.027
0.048
0.041
0.020
Val (V)
0.078
0.078
0.077 0.092 0.085 0.085
0.122
0.122
0.122
0.122
0.124
0.122
Trp (W)
0.000
0.000
0.000 0.007 0.007 0.007
0.014
0.014
0.014
0.014
0.014
0.014
Tyr (Y)
0.021
0.021
0.021 0.021 0.021 0.021
0.027
0.027
0.027
0.020
0.014
0.020