Raman spectroscopic analysis of DEA 1.1 canine RBC membrane glyco protein and its application in canine blood typing

Dog erythrocytic membrane antigen plays a major role for determining blood group. Structural and molecular characterization of erythrocytic membrane antigen improves the production of blood typing antisera, to study the auto antibody production in canine autoimmune haemolytic anemia. The proteins in the lipid domain arranged from the inside of the erythrocyte to the outside. The integral membrane proteins include membrane protein 3 visible in Coomassie Brilliant Blue-stained polyacrylamide gels. The erythrocyte cytoskeleton consists of spectrin, ankyrin, actin and protein 4.1 form a filamentous network under the lipid bilayer of erythroctic membrane. Most characteristic bands are associated with the CO =NH group referred to as amide A have NH stretching mostly found at 3500 cm -1 wave number. The amide B had NH stretching found at the region of 3100 cm -1 and amide I & III were used to estimate the secondary structure of proteins. Amide I mode which ranges from 1580 cm -1 to 1700 cm -1 and very sensitive to the backbone conformation and not affected by the side chains. Amide I band can be de convoluted with various sub-bands which directly correlate with various secondary structures The good intensity sharp peak at the level of 1468 cm -1 and 2034.694 cm -1 were taken for 2D analysis the CCD cts scale bar shows differences between DEA1.1 positive and negative dog erythrocytic membrane antigen. for and 3D analysis for identification of function group and β sheets structure symmetric of C=C, C=C functional group structure (C=H) functional group identified) and asymmetric (CH2)δ(CH3) identified. canine erythrocytic glycoprotein using raman spectroscopy and tried raman spectroscopy for blood grouping. The DEA 1.1 positive and negative glycoprotein showed significant differences in the composition of membrane glycoprotein in-depth