Publisher : Asian Australasian Association of Animal Production Societies
DOI : 10.5713/ajas.2011.11162
Title & Authors
Sialoglycoproteins of Mammalian Erythrocyte Membranes: A Comparative Study Sharma, Savita; Gokhale, Sadashiv M.;
The presence of sialoglycoproteins (SGPs) in the membranes from goat (Capra aegagrus hircus), buffalo (Bubalus bubalis bubalis) and pig (Sus scrofa domestica) erythrocytes was investigated by partial purification with a chloroform-methanol extraction method followed by Sodium dodecyl sulphate - Polyacrylamide gel electrophoresis in comparison to human (Homo sapiens) erythrocytes. The results show that mammalian erythrocytes possess clear differences in the SGPs numbers and molecular weights although all animals studied in this experiment are from the same class i.e. mammalia. The SGPs number in human, goat, buffalo and pig are four (PAS-1 to PAS-4), ten (PAS-GI to PAS-GX), seven (PAS-BI to PAS-BVII) and four (PAS-PI to PAS-IV) respectively as indicated by staining the polyacrylamide gel with sialoglycoprotein-specific Periodic acid-Schiff's (PAS) stain. The new SGPs could be observed only after the partial purification of membrane fractions named as PAS-HI with molecular weight (Mr) 190 kDa and PAS-HII 150 kDa in human, PAS-BIA in buffalo and PAS-PIA and PAS-PIVA in pig. The gels were also stained with Coomassie brilliant blue (CBB) and Silver stain to check the contamination of other membrane proteins in the purified fractions. The quantitative distribution of SGPs was also determined by densitometry. Present study indicates that there are some basic differences in mammalian erythrocyte membrane SGPs, especially with respect to their number and molecular weights indicating major structural variations.
A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry, The Journal of Membrane Biology, 2014, 247, 11, 1181
Barker, R. N. 1991. Electrophoretic analysis of erythrocyte membrane proteins and glycoproteins from different species. Comp. Haematol. Int. 1:155-160.
Chasis, J. A. and N. Mohandas. 1992. Red blood cell glycophorins. Blood 80:1869-1879.
Chaudhuri, A., V. Zbrzezna, C. Johnson, M. Nichols, P. Rubinsteinq, W. L. Marsh and A. O. Pogo. 1989. Purification and characterization of an erythrocyte membrane protein complex carrying Duffy blood group antigenicity. Possible receptor for Plasmodium vivax and Plasmodium knowlesi. J. Biol. Chem. 264:13770-13774.
Daniels, G. 1999. Functional aspects of red cell antigens. Blood Rev. 13:14-35.
Fairbanks, G., T. L. Steck and D. F. H. Wallach. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606-2617.
Fletcher, M. A., T. M. Lo and W. R. Graves. 1976. Immunochemical studies of infectious mononucleosis. V. Isolation and characterization of a glycoprotein from goat erythrocyte membranes. J. Immunol. 117:722-729.
Furthmayr, H., M. Tomita and V. T. Marchesi. 1975. Fractionation of the major sialoglycopeptides of the human red blood cell membrane. Biochem. Biophys. Res. Commun. 65:113-121.
Gratzer, W. B. 1981. The red cell membrane and its cytoskeleton. Biochem. J. 198:1-8.
Hamaguchi, H. and H. Cleve. 1972. Solubilization and comparative analysis of mammalian erythrocyte membrane glycoproteins. Biochem. Biophys. Res. Commun. 47:459-464.
Hanahan, D. J. and J. E. Ekholn. 1974. The preparation of red cell ghosts (membranes). Methods Enzymol. 31:168-172.
Herraez, A., J. C. Diez and J. Luque. 1992. Rat erythrocyte glycophorins can be isolated by the lithium diiodosalicylate method used for other glycophorins. Int. J. Biochem. 24:1705-1709.
Inaba, M. and Y. Maede. 1988. A new major transmembrane glycoprotein, gp155, in goat erythrocytes. J. Biol. Chem. 263:17763-17771.
Kakhniashvili, D. G., L. A. Bulla and S. R. Goodman. 2004. The human erythrocyte proteome. Mol. Cell. Proteomics 3:501-509.
Kornfeld, R. and S. Kornfeld. 1970. The structure of a phytohemagglutinin receptor site from human erythrocytes. J. Biol. Chem. 245:2536-2545.
Kumar, K. A., S. Singh and P. P. Babu. 2006. Studies on the glycoprotein modification in erythrocyte membrane during experimental cerebral malaria. Exp. Parasitol. 114:173-179.
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
Lowry, O. H., N. J. Rosebrough, A. L. Farr and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
Matei, H., L. Frentescu and Gh. Benga. 2000. Comparative studies of the protein composition of red blood cell membranes from eight mammalian species. J. Cell. Mol. Med. 4:270-276.
Murayama, J., M. Tomita and A. Hamada. 1982. Glycophorins of bovine erythrocyte membranes. Isolation and preliminary characterization of the major component. J. Biol. Chem. 91:1829-1836.
Pasini, E. M., H. U. Lutz, M. Mann and A. W. Thomas. 2010. Red blood cell (RBC) membrane proteomics - Part II: Comparative proteomics and RBC patho-physiology. J. Proteomics 73:421-435.
Steck, T. L. 1974. The organization of proteins in the human red blood cell membrane. J. Cell Biol. 62:1-19.
Spring, F. A. 2008. Characterization of blood-group-active erythrocyte membrane glycoproteins with human antiseras. Transfus. Med. 3:167-178.
Tanner, M. J. A. and D. H. Boxer. 1972. Separation and some properties of the major proteins of the human erythrocyte membrane. Biochem. J. 129:333-347.