Inter-protein bonding and other molecular interactions in hen egg white
Апстракт
The analysis of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) data, combined with the comparison of viscosity data corresponding to the, thin fraction of hell egg white and 2 mM purefied ovalbumin solution, showed that the thin fraction is a protein solution. Dissolution of the thick fraction of hen egg white in SDS and urea solutions followed by SDS-PAGE, in the presence or absence of P-mercaptoethanol, revealed that it is a protein gel. It was also found that the gel structure consists of the three-dimensional ovomucine-ovomucoid network (matrix) held together by SS bridges which captures the rest of the proteins (ovalbumin, conalbumin, etc). The captured proteins can also be interconnected by S-S bridges thus forming agglomerates or conglomerates, but they are predominantly held by weak electrostatic interactions, as demonstrated by the washing out and dissolving experiments. The matrix structure does not prevent denaturation of the captured proteins as indecated by the 50% ...decrease in turbidity following gel swelling by the addition of 1 part of an 8 M urea solution to 9 parts of the gel.
Кључне речи:
protein / gel / disulfide bond / bound water / denaturationИзвор:
Journal of the Serbian Chemical Society, 2000, 65, 3, 157-166Колекције
Институција/група
VinčaTY - JOUR AU - Vučković, M AU - Radojčić, Marija AU - Milosavljević, B.H. PY - 2000 UR - https://vinar.vin.bg.ac.rs/handle/123456789/2332 AB - The analysis of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) data, combined with the comparison of viscosity data corresponding to the, thin fraction of hell egg white and 2 mM purefied ovalbumin solution, showed that the thin fraction is a protein solution. Dissolution of the thick fraction of hen egg white in SDS and urea solutions followed by SDS-PAGE, in the presence or absence of P-mercaptoethanol, revealed that it is a protein gel. It was also found that the gel structure consists of the three-dimensional ovomucine-ovomucoid network (matrix) held together by SS bridges which captures the rest of the proteins (ovalbumin, conalbumin, etc). The captured proteins can also be interconnected by S-S bridges thus forming agglomerates or conglomerates, but they are predominantly held by weak electrostatic interactions, as demonstrated by the washing out and dissolving experiments. The matrix structure does not prevent denaturation of the captured proteins as indecated by the 50% decrease in turbidity following gel swelling by the addition of 1 part of an 8 M urea solution to 9 parts of the gel. T2 - Journal of the Serbian Chemical Society T1 - Inter-protein bonding and other molecular interactions in hen egg white VL - 65 IS - 3 SP - 157 EP - 166 UR - https://hdl.handle.net/21.15107/rcub_vinar_2332 ER -
@article{ author = "Vučković, M and Radojčić, Marija and Milosavljević, B.H.", year = "2000", abstract = "The analysis of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) data, combined with the comparison of viscosity data corresponding to the, thin fraction of hell egg white and 2 mM purefied ovalbumin solution, showed that the thin fraction is a protein solution. Dissolution of the thick fraction of hen egg white in SDS and urea solutions followed by SDS-PAGE, in the presence or absence of P-mercaptoethanol, revealed that it is a protein gel. It was also found that the gel structure consists of the three-dimensional ovomucine-ovomucoid network (matrix) held together by SS bridges which captures the rest of the proteins (ovalbumin, conalbumin, etc). The captured proteins can also be interconnected by S-S bridges thus forming agglomerates or conglomerates, but they are predominantly held by weak electrostatic interactions, as demonstrated by the washing out and dissolving experiments. The matrix structure does not prevent denaturation of the captured proteins as indecated by the 50% decrease in turbidity following gel swelling by the addition of 1 part of an 8 M urea solution to 9 parts of the gel.", journal = "Journal of the Serbian Chemical Society", title = "Inter-protein bonding and other molecular interactions in hen egg white", volume = "65", number = "3", pages = "157-166", url = "https://hdl.handle.net/21.15107/rcub_vinar_2332" }
Vučković, M., Radojčić, M.,& Milosavljević, B.H.. (2000). Inter-protein bonding and other molecular interactions in hen egg white. in Journal of the Serbian Chemical Society, 65(3), 157-166. https://hdl.handle.net/21.15107/rcub_vinar_2332
Vučković M, Radojčić M, Milosavljević B. Inter-protein bonding and other molecular interactions in hen egg white. in Journal of the Serbian Chemical Society. 2000;65(3):157-166. https://hdl.handle.net/21.15107/rcub_vinar_2332 .
Vučković, M, Radojčić, Marija, Milosavljević, B.H., "Inter-protein bonding and other molecular interactions in hen egg white" in Journal of the Serbian Chemical Society, 65, no. 3 (2000):157-166, https://hdl.handle.net/21.15107/rcub_vinar_2332 .