Determination of the Bacteriostatic Activity of Glycophorin Preparations from Red Blood Cell (RBC) Membranes of Yellow Tail and Red Sea Bream
Main Article Content
Abstract
Glycophorins (GPs) in red blood cell (RBC) membranes of carp (Cyprinus carpio L.) exhibit bacteriostatic activity against various gram-negative and gram-positive bacteria. To clarify the physiological activity of teleost fish GPs other than those from carp, we performed a sensitivity test using GP preparations from the RBC membranes of yellow tail and red sea bream. The sensitivity test for the growth of Micrococcus luteus was performed using the disc-plate method. These results suggested that the yellow tail and red sea bream GPs exhibit antibiotic activities.
Keywords:
teleost, yellow tail, red sea bream, red blood cell membranes, glycophorin, antibiotic activity
Article Details
How to Cite
AOKI, Takahiko.
Determination of the Bacteriostatic Activity of Glycophorin Preparations from Red Blood Cell (RBC) Membranes of Yellow Tail and Red Sea Bream.
Medical Research Archives, [S.l.], v. 9, n. 12, dec. 2021.
ISSN 2375-1924.
Available at: <https://esmed.org/MRA/mra/article/view/2613>. Date accessed: 25 apr. 2024.
doi: https://doi.org/10.18103/mra.v9i12.2613.
Section
Research Articles
The Medical Research Archives grants authors the right to publish and reproduce the unrevised contribution in whole or in part at any time and in any form for any scholarly non-commercial purpose with the condition that all publications of the contribution include a full citation to the journal as published by the Medical Research Archives.
References
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19. Dahr W, Moulds J, Baumeister G, Moulds M, Kiedrowski S, Hummel M. Altered membrane sialoglycoproteins in human erythrocites lacking the Gerbich blood group antigens. Bio. Chem. Hoppe-Seyler. 1985;366:201-211.
20. Lisowska E. Antigenic properties of human glycophorins – An update.
In The Molecular Immunology of Complex Carbohydrates – 2, 2001 (pp.155-169). Springer USA.
21. Michel F, Rudloff V. Isolation and characterization of the rainbow trout erythrocyte band-3 protein. European Journal of Biochemistry. 1989;181:181-187.
22. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry. 1951;193:265-275.
23. Wilson M, Bengtén E, Miller NW, Clem LW, Du Pasquier L, Warr GW. A novel chimeric Ig heavy chain from a teleost fish shares similarities to IgD. Proc. Natl. Acad. Sci. USA. 1997;94:4593-4597.
2. Blanchard D. Human red cell glycophorins: Biochemical and antigenic properties. Transfusion Medicine Reviews. 1990;4:170-186.
3. Chasis JA, Mohandas N. Red blood cell glycophorins. Blood. 1992;80:1869-1879.
4. Tanner MJA. Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Seminars in Hematology. 1993;30:34-57.
5. Yamashita T, Murayama J, Utsumi H, Hamada A. Structural studies of O-glycosidic oligosaccharide units of dog erythrocyte glycophorin. Biochim. Biophys. Acta. 1985;839:26-31.
6. Angel A-S, Grönberg G, Krotkiewski H, Lisowska E, Nilsson B. Structural analysis of the N-linked oligosaccharides from murine glycophorin. Arch. Biochem. Biophys. 1991; 291:76-88.
7. Murayama J-I, Utsumi H, Hamada A. Amino acid sequence of monkey erythrocyte glycophorin MK. Its amino acid sequence has a striking homology with that of human glycophorin A. Biochim. Biophys. Acta. 1989;999:273-280.
8. Krotkiewski H, The structure of glycophorins of animal erythrocytes. Glycoconj. J. 1988;5;35-48.
9. Watts C, Wheeler KP. Partial separation of a sodium-dependent transport system for amino acids in avian erythrocyte membranes. FEBS Letters. 1978;94:241-244.
10. Dockham PA, Vidaver GA. Comparison of human and pigeon erythrocyte membrane proteins by one- and two-dimensional gel electrophoresis. Comparative Biochemistry and Physiology Part B. 1987;87:171-177.
11. Aoki T, Fukai M, Ueno R. Glycoproteins in red cell membranes from carp and rainbow trout. Fisheries Science. 1996;62:498-499.
12. Aoki T, Chimura K, Nakao N, Mizuno Y. Isolation and characterization of glycophorin from carp red blood cell membranes. Membranes. 2014;4:491-508.
13. Aoki T, Chimura K, Sugiura H, Mizuno Y. Structure of a sialo-oligosaccharide from glycophorin in carp red blood cell membranes. Membranes. 2014;4:764-777.
14. Aoki T. A comprehensive review of our current understanding of red blood cell (RBC) glycoproteins. Membranes. 2017;7:56-74.
15. Aoki T, Inoue T. Glycophorin in red blood cell membranes of healthy and diseased carp, Cyprinus carpio L. Journal of Fish Diseases. 2011;34:573-576.
16. Dahr W, Beyreuther K, Steinbach, H, Gielen W, Krüger J. Structure of the Ss blood group antigens, Ⅱ. A methionine/threonine polymorphism within the N-terminal sequence of the Ss glycoprotein. Hoppe-Seyler Z. Physiol. Chem. 1980;361:895-906.
17. Prohaska R, Koerner TAW Jr, Armitage IM, Furthmayr H. Chemical and carbon-13 nuclear magnetic resonance studies of the blood group M and N active sialoglycopeptides from human glycophorin A. J. Biol. Chem. 1981;256:5781-5791.
18. Anstee DJ, Ridgwell K, Tanner MJA, Daniels GL, Parsons SF. Individuals lacking the Gerbich blood-group antigen have alterations in the human erythrocyte membrane sialoglycoproteins β and γ. Biochem. J. 1984;221:97-104.
19. Dahr W, Moulds J, Baumeister G, Moulds M, Kiedrowski S, Hummel M. Altered membrane sialoglycoproteins in human erythrocites lacking the Gerbich blood group antigens. Bio. Chem. Hoppe-Seyler. 1985;366:201-211.
20. Lisowska E. Antigenic properties of human glycophorins – An update.
In The Molecular Immunology of Complex Carbohydrates – 2, 2001 (pp.155-169). Springer USA.
21. Michel F, Rudloff V. Isolation and characterization of the rainbow trout erythrocyte band-3 protein. European Journal of Biochemistry. 1989;181:181-187.
22. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry. 1951;193:265-275.
23. Wilson M, Bengtén E, Miller NW, Clem LW, Du Pasquier L, Warr GW. A novel chimeric Ig heavy chain from a teleost fish shares similarities to IgD. Proc. Natl. Acad. Sci. USA. 1997;94:4593-4597.