Advanced SearchSearch Tips
Sialoglycoproteins of Mammalian Erythrocyte Membranes: A Comparative Study
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Sialoglycoproteins of Mammalian Erythrocyte Membranes: A Comparative Study
Sharma, Savita; Gokhale, Sadashiv M.;
  PDF(new window)
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.
Bubalus bubalis bubalis;Capra aegagrus hircus;Electrophoresis;Erythrocyte;Homo sapiens;Membrane sialoglycoproteins;Sus scrofa domestica;
 Cited by
A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry, The Journal of Membrane Biology, 2014, 247, 11, 1181  crossref(new windwow)
Barker, R. N. 1991. Electrophoretic analysis of erythrocyte membrane proteins and glycoproteins from different species. Comp. Haematol. Int. 1:155-160. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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. crossref(new window)

Hanahan, D. J. and J. E. Ekholn. 1974. The preparation of red cell ghosts (membranes). Methods Enzymol. 31:168-172. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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. crossref(new window)

Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. crossref(new window)

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. crossref(new window)

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. crossref(new window)

Steck, T. L. 1974. The organization of proteins in the human red blood cell membrane. J. Cell Biol. 62:1-19. crossref(new window)

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.