Change in carbohydrates of chicken and quail ovomucoids by gamma radiation

Radiation Physics and Chemistry

Volumn 54, Issue 3, 1999, Pages 285-290

  Lee, Young Keun ^a   Matsuhashi, Shinpei ^b   Kume, Tamikazu ^b  

^a Korea Atomic Energy Research Institute   (South Korea)

^b TAKASAKI ADVANCED RADIATION RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CONFORMATIONS; DEGRADATION; ENZYME INHIBITION; GAMMA RAYS; OXYGEN; RADIATION EFFECTS;

PROTEASE; TRYPSIN;

POLYSACCHARIDES;

CARBOHYDRATE; EGG WHITE; GLYCOPROTEIN; OLIGOSACCHARIDE; OVOMUCOID; TRYPSIN INHIBITOR;

ARTICLE; CARBOHYDRATE ANALYSIS; CHEMICAL STRUCTURE; CHICKEN; CONFORMATIONAL TRANSITION; DOSE RESPONSE; GAMMA RADIATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IMMUNOBLOTTING; IONIZING RADIATION; MOLECULAR WEIGHT; NONHUMAN; QUAIL; RADIATION DOSE; STRUCTURE ANALYSIS;

EID: 0033104591     PISSN: 0969806X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-806X(98)00234-5     Document Type: Article

References (19)

1. Dwek Raymond A. Glycobiology: toward understanding the function of sugars. Chem. Rev. 96:1996;683.
2. Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., Smith F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 28:1956;350.
3. Gu J., Matsuda T., Nakamura R., Ishiguro H., Ohkubo I., Sasaki M., Takahashi N. Chemical deglycosylation of hen ovomucoid: protective effect of carbohydrate moiety on tryptic hydrolysis and heat denaturation. J. Biochem. 106:1989;66.
4. Kato, K., Kohr, W.J., Laskowski, M. Jr, 1977. Evolution of avian ovomucoids. Regulatory proteolytic enzymes and their inhibitors. FEBS Federation of European Biochemical Societies' 11th Meeting, Copenhagen.
5. Kato Y., Matsuda T., Nakamura R. Change of the function of food protein by the aminocarbonyl reaction. New Food Indust. 37:1995;62.
6. Kato I., Schrode J., Kohr W.J., Laskowski M. Jr. Chicken ovomucoid: Determination of its amino acid sequence, determination of the trypsin reactive site and preparation of all three of its domains. Biochemistry. 26:1987;193.
7. Kondo M., Harada H., Sunada S., Yamaguchi T. Increased selectivity in the detection of glycoproteins on nitrocellulose membranes by washing with sodium hydroxide solution. Electrophoresis. 12:1991;685.
8. Kume T., Ishigaki I. Functional molecular size of trypsin inhibitors as determined by radiation inactivation analysis. Biochm. Biophy. Acta. 914:1987;101.
9. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680.
10. Matsuda T., Nakamura R. Molecular structure and immunological properties of food allergens. Trend Food Sci. 4:1994;289.
11. Matsuda T., Watanabe T., Nakamura R. Immunochemical studies in thermal denaturation of ovomucoid. Biochim. Biophy. Acta. 707:1982;121.
12. Niels, W.H., Roger, J.B., 1970. Manual on Radiation Dosimetry. Marcel Dekker Inc., New York.
13. Okada, S., 1970. K.I. Altman, G.G. Gerber, S. Okada (Ed.). Radiation Chemistry. Academic Press, New York.
14. Spinks, J.W.T., Woods, R.J., 1976. An Introduction to Radiation Chemistry. John Wiley and Sons, Inc., New York.
15. Towin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:1979;4350.
16. Waheed A., Salahuddin A. Isolation and characterization of a variant of ovomucoid. Biochem. J. 147:1975;139.
17. Watanabe K., Matsuda T., Sato Y. The secondary structure of ovomucoid and its domains as studied by circular dichroism. Biochim. Biophy. Acta. 667:1981;242.
18. Yamashita K., Kamerling J.P., Kobata A. Structural study of the carbohydrate moiety of the ovomucoid. J. Biol. Chem. 257:1982;12,809.
19. Yang J-S., Kim J-H., Matsuhashi S., Kume T. Changes in biochemical properties of ovomucoid by radiation. Rad. Phys. Chem. 48:(6):1996;731.