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-LY 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.
