A kinetic study of the mechanism of radiation induced agglomeration of ovalbumin in aqueous solution
Abstract
The effect of concentration on the protein radiolytic damage resulting in a change in molecular mass was measured in the concentration range from 0.2 to 2 mmol x dm(-3) ovalbumin in phosphate buffered solutions saturated with N2O. The electrophoretic analysis of samples on discontinuous SDS-polyacrylamide gets in the presence or absence of 5% beta -mercaptoethanol showed an expected result, i.e. that the protein scission did not take place in the absence of oxygen. Only ovalbumin agglomerates, bonded by covalent bonds other than S-S bridges, were observed. The G-value for the formation of ovalbumin agglomerates increased linearly from 1.1 to 2.4 by increasing the ovalbumin concentration from 0.2 to 2 mmol x dm-3. The result is interpreted as to be owing to the competition between ovalbumin agglomeration and some intramolecular reactions which did not lead to the change in the molecular mass. It was also found that the G-value is independent of irradiation dose rate. The result was rati...onalized as a kinetic evidence that the agglomeration is not a cross-linking process, i.e. it does not occur via recombination of the protein radicals produced in the interaction of ovalbumin and (OH)-O-. radical. The result suggested that the agglomeration takes place via the process of grafting, i.e. it occurs in the reaction of ovalbumin radical and an intact ovalbumin molecule. The time-resolved light scattering experiments provided an additional proof, supporting the reaction scheme of radiation-induced protein agglomeration. The biological consequences of the proposed mechanism of protein agglomeration are also discussed. (C) 2001 Elsevier Science Ltd. All rights reserved.
Keywords:
protein / ovalbumin / radiation / agglomeration / graftingSource:
Radiation Physics and Chemistry, 2001, 62, 4, 325-331
DOI: 10.1016/S0969-806X(01)00204-3
ISSN: 0969-806X
WoS: 000171686800004
Scopus: 2-s2.0-0034816640
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Institution/Community
VinčaTY - JOUR AU - Tuce, Z AU - Janata, E AU - Radojčić, Marija AU - Milosavljević, B.H. PY - 2001 UR - https://vinar.vin.bg.ac.rs/handle/123456789/2474 AB - The effect of concentration on the protein radiolytic damage resulting in a change in molecular mass was measured in the concentration range from 0.2 to 2 mmol x dm(-3) ovalbumin in phosphate buffered solutions saturated with N2O. The electrophoretic analysis of samples on discontinuous SDS-polyacrylamide gets in the presence or absence of 5% beta -mercaptoethanol showed an expected result, i.e. that the protein scission did not take place in the absence of oxygen. Only ovalbumin agglomerates, bonded by covalent bonds other than S-S bridges, were observed. The G-value for the formation of ovalbumin agglomerates increased linearly from 1.1 to 2.4 by increasing the ovalbumin concentration from 0.2 to 2 mmol x dm-3. The result is interpreted as to be owing to the competition between ovalbumin agglomeration and some intramolecular reactions which did not lead to the change in the molecular mass. It was also found that the G-value is independent of irradiation dose rate. The result was rationalized as a kinetic evidence that the agglomeration is not a cross-linking process, i.e. it does not occur via recombination of the protein radicals produced in the interaction of ovalbumin and (OH)-O-. radical. The result suggested that the agglomeration takes place via the process of grafting, i.e. it occurs in the reaction of ovalbumin radical and an intact ovalbumin molecule. The time-resolved light scattering experiments provided an additional proof, supporting the reaction scheme of radiation-induced protein agglomeration. The biological consequences of the proposed mechanism of protein agglomeration are also discussed. (C) 2001 Elsevier Science Ltd. All rights reserved. T2 - Radiation Physics and Chemistry T1 - A kinetic study of the mechanism of radiation induced agglomeration of ovalbumin in aqueous solution VL - 62 IS - 4 SP - 325 EP - 331 DO - 10.1016/S0969-806X(01)00204-3 ER -
@article{ author = "Tuce, Z and Janata, E and Radojčić, Marija and Milosavljević, B.H.", year = "2001", abstract = "The effect of concentration on the protein radiolytic damage resulting in a change in molecular mass was measured in the concentration range from 0.2 to 2 mmol x dm(-3) ovalbumin in phosphate buffered solutions saturated with N2O. The electrophoretic analysis of samples on discontinuous SDS-polyacrylamide gets in the presence or absence of 5% beta -mercaptoethanol showed an expected result, i.e. that the protein scission did not take place in the absence of oxygen. Only ovalbumin agglomerates, bonded by covalent bonds other than S-S bridges, were observed. The G-value for the formation of ovalbumin agglomerates increased linearly from 1.1 to 2.4 by increasing the ovalbumin concentration from 0.2 to 2 mmol x dm-3. The result is interpreted as to be owing to the competition between ovalbumin agglomeration and some intramolecular reactions which did not lead to the change in the molecular mass. It was also found that the G-value is independent of irradiation dose rate. The result was rationalized as a kinetic evidence that the agglomeration is not a cross-linking process, i.e. it does not occur via recombination of the protein radicals produced in the interaction of ovalbumin and (OH)-O-. radical. The result suggested that the agglomeration takes place via the process of grafting, i.e. it occurs in the reaction of ovalbumin radical and an intact ovalbumin molecule. The time-resolved light scattering experiments provided an additional proof, supporting the reaction scheme of radiation-induced protein agglomeration. The biological consequences of the proposed mechanism of protein agglomeration are also discussed. (C) 2001 Elsevier Science Ltd. All rights reserved.", journal = "Radiation Physics and Chemistry", title = "A kinetic study of the mechanism of radiation induced agglomeration of ovalbumin in aqueous solution", volume = "62", number = "4", pages = "325-331", doi = "10.1016/S0969-806X(01)00204-3" }
Tuce, Z., Janata, E., Radojčić, M.,& Milosavljević, B.H.. (2001). A kinetic study of the mechanism of radiation induced agglomeration of ovalbumin in aqueous solution. in Radiation Physics and Chemistry, 62(4), 325-331. https://doi.org/10.1016/S0969-806X(01)00204-3
Tuce Z, Janata E, Radojčić M, Milosavljević B. A kinetic study of the mechanism of radiation induced agglomeration of ovalbumin in aqueous solution. in Radiation Physics and Chemistry. 2001;62(4):325-331. doi:10.1016/S0969-806X(01)00204-3 .
Tuce, Z, Janata, E, Radojčić, Marija, Milosavljević, B.H., "A kinetic study of the mechanism of radiation induced agglomeration of ovalbumin in aqueous solution" in Radiation Physics and Chemistry, 62, no. 4 (2001):325-331, https://doi.org/10.1016/S0969-806X(01)00204-3 . .