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Effect of Gamma-Irradiation on the Molecular Properties of Blood Plasma Proteins

  • Song, Kyung-Bin (Department of Food Science and Technology, Chungnam National University) ;
  • Lee, Seunghwan (Department of Food Science and Technology, Chungnam National University) ;
  • Lee, Seunghyun (Department of Food Science and Technology, Chungnam National University)
  • Published : 2002.06.01

Abstract

Blood products from slaughterhouses that are not hygienically prepared for disposal or food consumption pose a human health hazard. Gamma irradiation is an effective method for sterilization of blood products, but may introduce changes in the molecular characteristics of proteins. This study evaluated the effects of irradiation on animal plasma proteins. Bovine and porcine blood was obtained from a slaughterhouse and the plasma proteins purified and lyophilized. The secondary structure and molecular weight distribution of the plasma protein solutions and powders were examined after ${\gamma}$-irradiation at 1, 5, 7 and 10 kGy. Gamma-irradiation affected the molecular properties of the protein solutions, but not the protein powders. Circular dichroism and sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies showed that increased doses of ${\gamma}$-irradiation decrease the ordered structure of plasma proteins in solution, and cause initial fragmentation of the polypeptide chains and subsequent aggregation.

References

  1. Mahrour A, Lacroix M, Nketsa-Tabiri J, Calderon N, Gagnon M. 1998. Antimicrobial properties of natural substances in irradiated fresh pourtry. Radiat Phys Chem 52: 81-84 https://doi.org/10.1016/S0969-806X(98)00079-6
  2. Foley DM, Dufour A, Rodriguez L, Caporaso F, Prakash A. 2002. Reduction of Escherichia coli 0157: H7 in shredded iceberg lettuce by chlorination and gamma-irradiation. Radiat Phys Chem 63: 391-396 https://doi.org/10.1016/S0969-806X(01)00530-8
  3. Schuessler H, Schilling K. 1984. Oxygen effect in the radiolysis of proteins. Int J Radiat Biol 45: 267-281 https://doi.org/10.1080/09553008414550381
  4. Garrison WM. 1987. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem Rev 87: 381- 398 https://doi.org/10.1021/cr00078a006
  5. Davies KJA, Delsignore ME. 1987. Protein damage and degradation by oxygen radicals III. Modification of secondary structure and tertiary structure. J Biol Chem 262: 9908- 9913
  6. Filali-Mouhim A, Audette M, St-Louis M, Thauvette L, Denoroy L, Penin F, Chen X, Rouleau N, Le Caer JP, Rossier J, Potier M, Le Maire M. 1997. Lysozyme fragmentation induced by radiolysis. Int J Radiat Biol 72: 63- 70 https://doi.org/10.1080/095530097143545
  7. Woods RJ, Pickaev AK. 1994. Applied radiation chemistry. John Wiley and Sons, New York
  8. Kempner ES. 1993. Damage to proteins due to the direct action of ionizing radiation. Quart Rev Biophys 26: 27-48 https://doi.org/10.1017/S0033583500003954
  9. Puchala M, Schuessler H. 1993. Oxygen effect in the radiolysis of proteins. Int J Radiat Biol 64: 149-156 https://doi.org/10.1080/09553009314551231
  10. Kume T, Matsuda T. 1995. Changes in structural and antigenic properties of proteins by radiation. Radiat Phys Chem 46: 225-231 https://doi.org/10.1016/0969-806X(95)00017-R
  11. Cho Y, Song KB. 1997. Effect of chaotropic salt on the secondary structure of pig skin gelatin. Biosci Biotech Biochem 61: 1194-1195 https://doi.org/10.1271/bbb.61.1194
  12. Lee MJ, Song KB. 1997. Purification of streptodornase from Streptococcus equisimilis and its DNA-induced conformational change. Biochem Biophys Res Comm 230: 13-15 https://doi.org/10.1006/bbrc.1996.5875
  13. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 https://doi.org/10.1038/227680a0
  14. Raeker MO, Johnson LA. 1995. Thermal and functional properties of bovine blood plasma and egg white proteins. J Food Sci 60: 685-690 https://doi.org/10.1111/j.1365-2621.1995.tb06206.x
  15. Park E, Lee H, Song KB. 1996. Characterization of plasma proteins from bloods of slaughtered cow and pig and utilization of the proteins as adhesives. Agric Chem Biotech 39(2): 123-126
  16. Cho Y, Yang J, Song KB. 1999. Effect of ascorbic acid and protein concentration on the molecular weight profile of BSA and $\beta$-lactoglobulin by $\gamma$-irradiation. Food Research Int 32(7): 515-519 https://doi.org/10.1016/S0963-9969(99)00127-1
  17. Le Maire M, Thauvette L, De Foresta B, Viel A, Beauregard G, Potier M. 1990. Effects of ionizing radiations on proteins. Biochem J 267: 431-439 https://doi.org/10.1042/bj2670431
  18. Cho Y, Song KB. 1999. Effect of $\gamma$-irradiation on the physicochemical properties of soy protein isolate and whey protein concentrate. Korean J Food Sci Technol 31: 1488- 1494
  19. Wolff SP, Garner A, Dean RT. 1986. Free radicals, lipids and protein degradation. Trends Biochem Sci 11: 27-31 https://doi.org/10.1016/0968-0004(86)90228-8
  20. Stevens CO, Sauberlich HE, Bergstrom GR. 1967. Radiation- produced aggregation and inactivation in egg white lysozyme. J Biol Chem 242: 1821-1826
  21. Cho Y, Song KB. 2000. Effect of $\gamma$-irradiation on the molecular properties of BSA and $\beta$-lactoglobulin. J Biochem Mol Biol 33: 133-137
  22. Moon S, Song KB. 2001. Effect of gamma-irradiation on the molecular properties of ovalbumin and ovomucoid and protection by ascorbic acid. Food Chem 74: 85-89 https://doi.org/10.1016/S0308-8146(01)00102-9

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