Chemical modification of beta-lactoglobulin by quinones
Hemijske modifikacije β-laktoglobulina hinonima
2003
Authors
Novaković, Irena T.Vujčić, Zoran
Božić, Tatjana T.
Božić, Nataša
Milosavic, N
Sladić, Dušan
Article (Published version)
Metadata
Show full item recordAbstract
The avarone/avarol quinone/hydroquinone couple. as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of beta-lactogglobulin. isolated from cow milk by avarone, its model compound 2-tert-butyl-1,4-benzoquinone. and several of their alkylthio derivatives were studied. The techniques applied for as-saying the modifications were: UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of die reaction of beta-lactoglobulin with the quinones.
Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima pokazuje da su amino grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.
Keywords:
avarone / quinone / quinone / β-lactoglobulin / beta-lactoglobulin / covalent modification / covalent modificationSource:
Journal of the Serbian Chemical Society, 2003, 68, 4-5, 243-248Publisher:
- Serbian Chemical Soc, Belgrade
DOI: 10.2298/JSC0305243N
ISSN: 0352-5139
WoS: 000183423800002
Scopus: 2-s2.0-0037498109
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Novaković, Irena T. AU - Vujčić, Zoran AU - Božić, Tatjana T. AU - Božić, Nataša AU - Milosavic, N AU - Sladić, Dušan PY - 2003 UR - https://cherry.chem.bg.ac.rs/handle/123456789/552 AB - The avarone/avarol quinone/hydroquinone couple. as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of beta-lactogglobulin. isolated from cow milk by avarone, its model compound 2-tert-butyl-1,4-benzoquinone. and several of their alkylthio derivatives were studied. The techniques applied for as-saying the modifications were: UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of die reaction of beta-lactoglobulin with the quinones. AB - Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima 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 - Chemical modification of beta-lactoglobulin by quinones T1 - Hemijske modifikacije β-laktoglobulina hinonima VL - 68 IS - 4-5 SP - 243 EP - 248 DO - 10.2298/JSC0305243N ER -
@article{ author = "Novaković, Irena T. and Vujčić, Zoran and Božić, Tatjana T. and Božić, Nataša and Milosavic, N and Sladić, Dušan", year = "2003", abstract = "The avarone/avarol quinone/hydroquinone couple. as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of beta-lactogglobulin. isolated from cow milk by avarone, its model compound 2-tert-butyl-1,4-benzoquinone. and several of their alkylthio derivatives were studied. The techniques applied for as-saying the modifications were: UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of die reaction of beta-lactoglobulin with the quinones., Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima 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 = "Chemical modification of beta-lactoglobulin by quinones, Hemijske modifikacije β-laktoglobulina hinonima", volume = "68", number = "4-5", pages = "243-248", doi = "10.2298/JSC0305243N" }
Novaković, I. T., Vujčić, Z., Božić, T. T., Božić, N., Milosavic, N.,& Sladić, D.. (2003). Chemical modification of beta-lactoglobulin by quinones. in Journal of the Serbian Chemical Society Serbian Chemical Soc, Belgrade., 68(4-5), 243-248. https://doi.org/10.2298/JSC0305243N
Novaković IT, Vujčić Z, Božić TT, Božić N, Milosavic N, Sladić D. Chemical modification of beta-lactoglobulin by quinones. in Journal of the Serbian Chemical Society. 2003;68(4-5):243-248. doi:10.2298/JSC0305243N .
Novaković, Irena T., Vujčić, Zoran, Božić, Tatjana T., Božić, Nataša, Milosavic, N, Sladić, Dušan, "Chemical modification of beta-lactoglobulin by quinones" in Journal of the Serbian Chemical Society, 68, no. 4-5 (2003):243-248, https://doi.org/10.2298/JSC0305243N . .