Protein covalent modification of biologically active quinones
Kovalentne modifikacije proteina biološki aktivnim hinonima

2004
Authors
Sladić, Dušan
Novaković, Irena

Vujčić, Zoran

Božić, Tatjana T.

Božić, Nataša

Milić, Dragana

Šolaja, Bogdan

Gašić, Miroslav J.
Article (Published version)
Metadata
Show full item recordAbstract
The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of β-lactoglobulin by avarone and its derivatives as well as by the synthetic steroidal quinone 2,5(10)-estradiene- 1,4,17-trione and its derivatives were studied. The techniques for studying chemical modification of β-lactoglobulin by quinones were: UV/Vis spectrophotometry, SDS PAGE and isoelectrofocusing. SDS PAGE results suggest that polymerization of the protein occurs. It could be seen that the protein of 18 kD gives the bands of 20 kD, 36 kD, 40 kD, 45 kD, 64 kD and 128 kD depending on modification agent. The shift of the pI of the protein (5.4) upon modification toward lower values (from pI 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of β-lactoglobulin with the quinones.
Hinonsko/hidrohinonski par avaron/avarol pokazuje značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina avaronom, sintetičkim steroidnim hinonom 2,5(10)-estradien-1,4,17-trionom i njihovim derivatima. Tehnike za praćenje hemijske modifikacije bile su: UV/Vis spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultati SDS PAGE ukazuju da se dešava polimerizacija proteina.Može se videti da protein od 18 kD daje trake od 20 kD, 36 kD, 40 kD, 45 kD, 64 kD i 128 kD u zavisnosti od agensa za modifikaciju. Pomeranje pI vrednosti proteina (5,4) nakon modifikacije ka nižim vrednostima (od pI 5,0 do 5,3) pokazuje da su amino-grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.
Keywords:
quinone / avarone / steroidal quinones / β-lactoglobulin / covalent modificationSource:
Journal of the Serbian Chemical Society, 2004, 69, 11, 901-907Publisher:
- Serbian Chemical Society
Funding / projects:
- Project MESTD, br. 1586
DOI: 10.2298/JSC0411901S
ISSN: 0352-5139
WoS: 000226120300009
Scopus: 2-s2.0-31544482774
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IHTMTY - JOUR AU - Sladić, Dušan AU - Novaković, Irena AU - Vujčić, Zoran AU - Božić, Tatjana T. AU - Božić, Nataša AU - Milić, Dragana AU - Šolaja, Bogdan AU - Gašić, Miroslav J. PY - 2004 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/138 AB - The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of β-lactoglobulin by avarone and its derivatives as well as by the synthetic steroidal quinone 2,5(10)-estradiene- 1,4,17-trione and its derivatives were studied. The techniques for studying chemical modification of β-lactoglobulin by quinones were: UV/Vis spectrophotometry, SDS PAGE and isoelectrofocusing. SDS PAGE results suggest that polymerization of the protein occurs. It could be seen that the protein of 18 kD gives the bands of 20 kD, 36 kD, 40 kD, 45 kD, 64 kD and 128 kD depending on modification agent. The shift of the pI of the protein (5.4) upon modification toward lower values (from pI 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of β-lactoglobulin with the quinones. AB - Hinonsko/hidrohinonski par avaron/avarol pokazuje značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina avaronom, sintetičkim steroidnim hinonom 2,5(10)-estradien-1,4,17-trionom i njihovim derivatima. Tehnike za praćenje hemijske modifikacije bile su: UV/Vis spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultati SDS PAGE ukazuju da se dešava polimerizacija proteina.Može se videti da protein od 18 kD daje trake od 20 kD, 36 kD, 40 kD, 45 kD, 64 kD i 128 kD u zavisnosti od agensa za modifikaciju. Pomeranje pI vrednosti proteina (5,4) nakon modifikacije ka nižim vrednostima (od pI 5,0 do 5,3) pokazuje da su amino-grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima. PB - Serbian Chemical Society T2 - Journal of the Serbian Chemical Society T1 - Protein covalent modification of biologically active quinones T1 - Kovalentne modifikacije proteina biološki aktivnim hinonima VL - 69 IS - 11 SP - 901 EP - 907 DO - 10.2298/JSC0411901S ER -
@article{ author = "Sladić, Dušan and Novaković, Irena and Vujčić, Zoran and Božić, Tatjana T. and Božić, Nataša and Milić, Dragana and Šolaja, Bogdan and Gašić, Miroslav J.", year = "2004", abstract = "The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of β-lactoglobulin by avarone and its derivatives as well as by the synthetic steroidal quinone 2,5(10)-estradiene- 1,4,17-trione and its derivatives were studied. The techniques for studying chemical modification of β-lactoglobulin by quinones were: UV/Vis spectrophotometry, SDS PAGE and isoelectrofocusing. SDS PAGE results suggest that polymerization of the protein occurs. It could be seen that the protein of 18 kD gives the bands of 20 kD, 36 kD, 40 kD, 45 kD, 64 kD and 128 kD depending on modification agent. The shift of the pI of the protein (5.4) upon modification toward lower values (from pI 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of β-lactoglobulin with the quinones., Hinonsko/hidrohinonski par avaron/avarol pokazuje značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina avaronom, sintetičkim steroidnim hinonom 2,5(10)-estradien-1,4,17-trionom i njihovim derivatima. Tehnike za praćenje hemijske modifikacije bile su: UV/Vis spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultati SDS PAGE ukazuju da se dešava polimerizacija proteina.Može se videti da protein od 18 kD daje trake od 20 kD, 36 kD, 40 kD, 45 kD, 64 kD i 128 kD u zavisnosti od agensa za modifikaciju. Pomeranje pI vrednosti proteina (5,4) nakon modifikacije ka nižim vrednostima (od pI 5,0 do 5,3) pokazuje da su amino-grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.", publisher = "Serbian Chemical Society", journal = "Journal of the Serbian Chemical Society", title = "Protein covalent modification of biologically active quinones, Kovalentne modifikacije proteina biološki aktivnim hinonima", volume = "69", number = "11", pages = "901-907", doi = "10.2298/JSC0411901S" }
Sladić, D., Novaković, I., Vujčić, Z., Božić, T. T., Božić, N., Milić, D., Šolaja, B.,& Gašić, M. J.. (2004). Protein covalent modification of biologically active quinones. in Journal of the Serbian Chemical Society Serbian Chemical Society., 69(11), 901-907. https://doi.org/10.2298/JSC0411901S
Sladić D, Novaković I, Vujčić Z, Božić TT, Božić N, Milić D, Šolaja B, Gašić MJ. Protein covalent modification of biologically active quinones. in Journal of the Serbian Chemical Society. 2004;69(11):901-907. doi:10.2298/JSC0411901S .
Sladić, Dušan, Novaković, Irena, Vujčić, Zoran, Božić, Tatjana T., Božić, Nataša, Milić, Dragana, Šolaja, Bogdan, Gašić, Miroslav J., "Protein covalent modification of biologically active quinones" in Journal of the Serbian Chemical Society, 69, no. 11 (2004):901-907, https://doi.org/10.2298/JSC0411901S . .