Protein covalent modification by biologically active quinones
Kovalentne modifikacije proteina biološki aktivnim hinonima
2004
Autori
Sladić, DušanNovaković, Irena T.
Vujčić, Zoran
Božić, Tatjana T.
Božić, Nataša
Milić, Dragana
Šolaja, Bogdan A.
Gasic, MJ
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of beta-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 beta-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 pl of the protein (5.4) upon modification toward lower values (from pl 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of beta-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.
Ključne reči:
quinone / avarone / avarone / steroidal quinones / steroidal quinones / β-lactoglobulin / beta-lactoglobulin / covalent modification / covalent modificationIzvor:
Journal of the Serbian Chemical Society, 2004, 69, 11, 901-907Izdavač:
- Serbian Chemical Soc, Belgrade
DOI: 10.2298/JSC0411901S
ISSN: 0352-5139
WoS: 000226120300009
Scopus: 2-s2.0-31544482774
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Sladić, Dušan AU - Novaković, Irena T. AU - Vujčić, Zoran AU - Božić, Tatjana T. AU - Božić, Nataša AU - Milić, Dragana AU - Šolaja, Bogdan A. AU - Gasic, MJ PY - 2004 UR - https://cherry.chem.bg.ac.rs/handle/123456789/678 AB - The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of beta-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 beta-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 pl of the protein (5.4) upon modification toward lower values (from pl 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of beta-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 Soc, Belgrade T2 - Journal of the Serbian Chemical Society T1 - Protein covalent modification by 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 T. and Vujčić, Zoran and Božić, Tatjana T. and Božić, Nataša and Milić, Dragana and Šolaja, Bogdan A. and Gasic, MJ", year = "2004", abstract = "The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of beta-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 beta-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 pl of the protein (5.4) upon modification toward lower values (from pl 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of beta-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 Soc, Belgrade", journal = "Journal of the Serbian Chemical Society", title = "Protein covalent modification by biologically active quinones, Kovalentne modifikacije proteina biološki aktivnim hinonima", volume = "69", number = "11", pages = "901-907", doi = "10.2298/JSC0411901S" }
Sladić, D., Novaković, I. T., Vujčić, Z., Božić, T. T., Božić, N., Milić, D., Šolaja, B. A.,& Gasic, M.. (2004). Protein covalent modification by biologically active quinones. in Journal of the Serbian Chemical Society Serbian Chemical Soc, Belgrade., 69(11), 901-907. https://doi.org/10.2298/JSC0411901S
Sladić D, Novaković IT, Vujčić Z, Božić TT, Božić N, Milić D, Šolaja BA, Gasic M. Protein covalent modification by biologically active quinones. in Journal of the Serbian Chemical Society. 2004;69(11):901-907. doi:10.2298/JSC0411901S .
Sladić, Dušan, Novaković, Irena T., Vujčić, Zoran, Božić, Tatjana T., Božić, Nataša, Milić, Dragana, Šolaja, Bogdan A., Gasic, MJ, "Protein covalent modification by biologically active quinones" in Journal of the Serbian Chemical Society, 69, no. 11 (2004):901-907, https://doi.org/10.2298/JSC0411901S . .