Investigation of the influence of gamma-irradiation and freezing on the thermodenaturation of placental human serum albumin by the method of dsc
Keywords:
placental albumin, gamma-irradiation, differential scanning calorimetry, denaturation
Abstract
In the paper the influence of various doses of gamma-irradiation (60-10000 Gy) on the process of the
denaturation of placental human serum albumin was investigated by the method of differential scanning
calorimetry (DSC). The combined affect of radiation and freezing down to the temperature of liquid
nitrogen on serum albumin in solution was carried out. The samples was irradiated at room temperature
on gamma-apparatus «Issledovatel» by Co60 gamma-quanta on power of the exhibition dose of 120 R/min. In the result of the study it was found that gamma-irradiation of placental albumin led to the loosening of macromolecules obviously evinced already at the dose of 1729 Gy and subsequent destruction of their structure. The lowering of cooperative processes at melting begins at low doses of radiation (60 Gy). It was showed that the cooling of albumin solutions down to the temperature of liquid nitrogen both before and after irradiation introduces the additional contribution to destructive processes taking place with albumin macromolecules.
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References
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20. Moon S. Effect of γ-irradiation on the molecular properties of egg white proteins / S. Moon, K. B. Song // Food. Sci. Biotechnol. – 2000. – V. 9. – P. 239–242.
21. Michnik A.Thermal stability of bovine serum albumin DSC study / A. Michnik // Journal of Thermal Analysis and Calorimetry. – 2003. – V. 71. – P. 509–519.
22. Gaber M. H. Effect of -Irradiation on the Molecular Properties of Bovine Serum Albumin / M. H. Gaber // Journal of Bioscience and Bioengineering. – 2005. – V. 100, №. 2. – P. 203–206.
2. Delincee H. Protein aggregation in foods models: effect of -irradiation and lipid oxidation / H. Delincee, P. Pushpa // Journal of Food Processing and Preservation. – 1981. – V. 5. – P. 145–159.
3. The effect of irradiation on technological properties and protein solubility of broiler chicken meat / J. Zabielski, J. Kijowski, W. Fiszer, J. Niewiarowicz // Sci. Food Agric. – 1984. – V. 35. – P. 662–670.
4. Nisizawa M. Radiation induced sol-gel transition of protein: effect of radiation on amino-acid composition and viscosity / M. J. Nisizawa // Appl. Polym. Sci. – 1988. – V. 36. – P. 979–981.
5. Bernofsky C. Biochemistry of myoglobin. VI. The effect of low dosage gamma irradiation on beef myoglobin / C. Bernofsky, J. B. Fox Jr, B. S. Schweigert // Arch. Biochem. Biophys. – 1959. – V. 80. – P. 9–21.
6. Ambe K. S. Radiation damadge to cytochrome C and hemoglobin / K. S. Ambe, U. S. Kumta, A. I. Tappel // Radiat. Res. – 1961. – V. 15. – P. 709–719.
7. Brown W. D. γ-irradiation of purified myoglobins. 1. Effect on physicochemical properties / W. D. Brown, J.-H. Argiroudi Akoyunoglou // Arch. Biochem. Biophys. – 1964. – V. 107. – P. 239–245.
8. Puchała M. γ-irradiation of aquas solutions of human hemoglobin in atmospheres of air and argon / M. Puchała, Z. Szweda-Lewandowska, W. Leyko // Radiat. Res. – 1979. – V. 78. – P. 379–389.
9. Witburn K. D. Interaction of radiation-generated radicals with myoglobin in aquas solutions - II. / K. D. Witburn, M. Z. Hoffman Radiat. Phys. Chem. – 1984. –V. 23. – P. 271–278.
10. Состояние белков сыворотки кордовой крови после замораживания / Э. О. Нардид, Е. Д. Розанова, Л. В. Цымбал [и др.] // Биофизика. – 2009. – Т. 54, Вып. 5. – С. 881–886. /Sostojanie belkov syvorotki kordovoj krovi posle zamorazhivanija / Je. O. Nardid, E. D. Rozanova, L. V. Cymbal [i dr.] // Biofizika. – 2009. – T. 54, Vyp. 5. – S. 881–886./
11. Ma C. Y. Studies on thermal denaturation of oat globulin by differential scanning calorimetry / C. Y. Ma, V.R. Harwalkar // J. Food Sci. – 1988. – V. 53. – V. 531–534.
12. Liu T. X. Thermal denaturation and heat induced gelation properties of -lactoglobulin. Effects of some chemical parameters / T. X. Liu, P. Relkin // Thermochim. Acta. – 1994. – V. 243. – P. 387–403.
13. Relkin P. Differential scanning calorimetry: a useful tool for studying protein denaturation / P. Relkin // Thermochim. Acta. – 1994. – V. 243. – P. 371–386.
14. Зинченко А. В. Сравнительное микрокалориметрическое плавление гемоглобина из донорской и кордовой крови до и после низкотемпературного воздействия / А. В. Зинченко, А. С. Соловьева // Проблемы криобиологии. – 2000. – № 1. – С. 32–35. /Zinchenko A. V. Sravnitel'noe mikrokalorimetricheskoe plavlenie gemoglobina iz donorskoj i kordovoj krovi do i posle nizkotemperaturnogo vozdejstvija / A. V. Zinchenko, A. S. Solov'eva // Problemy kriobiologii. – 2000. – № 1. – S. 32–35./
15. Переход ДНК в компактное состояние при связывании с ионами меди в растворах криопротекторов / Е. В. Хакл, С. В. Корнилова, А. В. Зинченко [и др.] // Проблемы криобиологии. – 1998. – № 3. – С. 67–69. /Perehod DNK v kompaktnoe sostojanie pri svjazyvanii s ionami medi v rastvorah krioprotektorov / E. V. Hakl, S. V. Kornilova, A. V. Zinchenko [i dr.] // Problemy kriobiologii. – 1998. – № 3. – S. 67–69./
16. Хенли Э. Радиационная химия / Э. Хенли, Э. Джонсон. – М.: Атомиздат, 1974. – 415 с. /Henli Je. Radiacionnaja himija / Je. Henli, Je. Dzhonson. – M.: Atomizdat, 1974. – 415 s./
17. Effect of UVC radiation on conformational restructuring of human serum albumin / A. Michnik, K. Michalik, Z. Drzazga // Journal of Photochemistry and Photohiology B: Biology. – 2008. – V. 90. – P. 170–178.
18. Исследование влияния -облучения на структуру бычьего сывороточного альбумина методом спиновых меток / О. А. Горобченко, О. Т. Николов, О. А. Нардид // Прикладная радиоэлектроника. – 2004. – Т. 2, № 1. – C. 84–87. /Issledovanie vlijanija -obluchenija na strukturu bych'ego syvorotochnogo al'bumina metodom spinovyh metok / O. A. Gorobchenko, O. T. Nikolov, O. A. Nardid // Prikladnaja radiojelektronika. – 2004. – T. 2, № 1. – C. 84–87./
19. Conformation transitions of blood proteins under influence of physical factors on microwave dielectric method / O. A. Gorobchenko, O. T. Nikolov, S. V. Gatash // Journal of Quantitative Spectroscopy & Radiative Transfer. – 2006. – V. 102. – P. 18–24.
20. Moon S. Effect of γ-irradiation on the molecular properties of egg white proteins / S. Moon, K. B. Song // Food. Sci. Biotechnol. – 2000. – V. 9. – P. 239–242.
21. Michnik A.Thermal stability of bovine serum albumin DSC study / A. Michnik // Journal of Thermal Analysis and Calorimetry. – 2003. – V. 71. – P. 509–519.
22. Gaber M. H. Effect of -Irradiation on the Molecular Properties of Bovine Serum Albumin / M. H. Gaber // Journal of Bioscience and Bioengineering. – 2005. – V. 100, №. 2. – P. 203–206.
Cited
How to Cite
ZinchenkoА. V., GorobchenkoО. А., NardidО. А., & NikolovО. T. (1). Investigation of the influence of gamma-irradiation and freezing on the thermodenaturation of placental human serum albumin by the method of dsc. Biophysical Bulletin, 1(29). Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/2351
Section
Action of physical agents on biological objects
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