Chemical modification of β-lactoglobulin by quinines
Hemijske modifikacije β-laktoglobulina hinonima
2003
Аутори
Novaković, IrenaVujčić, Zoran
Božić, Tatjana T.
Božić, Nataša
Milosavić, Nenad B.
Sladić, Dušan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The avarone/avarol quinone/hydroquinone couple, as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of β-lactoglobulin, 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 assaying 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 the reaction of β-lactoglobulin with the quinines.
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.
Кључне речи:
avarone / quinone / β-lactoglobulin / covalent modificationИзвор:
Journal of the Serbian Chemical Society, 2003, 68, 4-5, 243-248Издавач:
- Serbian Chemical Society
DOI: 10.2298/JSC0305243N
ISSN: 0352-5139
WoS: 000183423800002
Scopus: 2-s2.0-0037498109
Институција/група
IHTMTY - JOUR AU - Novaković, Irena AU - Vujčić, Zoran AU - Božić, Tatjana T. AU - Božić, Nataša AU - Milosavić, Nenad B. AU - Sladić, Dušan PY - 2003 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/118 AB - The avarone/avarol quinone/hydroquinone couple, as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of β-lactoglobulin, 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 assaying 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 the reaction of β-lactoglobulin with the quinines. 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 Society T2 - Journal of the Serbian Chemical Society T1 - Chemical modification of β-lactoglobulin by quinines T1 - Hemijske modifikacije β-laktoglobulina hinonima VL - 68 IS - 4-5 SP - 243 EP - 248 DO - 10.2298/JSC0305243N ER -
@article{ author = "Novaković, Irena and Vujčić, Zoran and Božić, Tatjana T. and Božić, Nataša and Milosavić, Nenad B. 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 β-lactoglobulin, 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 assaying 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 the reaction of β-lactoglobulin with the quinines., 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 Society", journal = "Journal of the Serbian Chemical Society", title = "Chemical modification of β-lactoglobulin by quinines, Hemijske modifikacije β-laktoglobulina hinonima", volume = "68", number = "4-5", pages = "243-248", doi = "10.2298/JSC0305243N" }
Novaković, I., Vujčić, Z., Božić, T. T., Božić, N., Milosavić, N. B.,& Sladić, D.. (2003). Chemical modification of β-lactoglobulin by quinines. in Journal of the Serbian Chemical Society Serbian Chemical Society., 68(4-5), 243-248. https://doi.org/10.2298/JSC0305243N
Novaković I, Vujčić Z, Božić TT, Božić N, Milosavić NB, Sladić D. Chemical modification of β-lactoglobulin by quinines. in Journal of the Serbian Chemical Society. 2003;68(4-5):243-248. doi:10.2298/JSC0305243N .
Novaković, Irena, Vujčić, Zoran, Božić, Tatjana T., Božić, Nataša, Milosavić, Nenad B., Sladić, Dušan, "Chemical modification of β-lactoglobulin by quinines" in Journal of the Serbian Chemical Society, 68, no. 4-5 (2003):243-248, https://doi.org/10.2298/JSC0305243N . .