Chemical modification of β-lactoglobulin by quinines
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...
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Serbian Chemical Society
2003-01-01
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| Series: | Journal of the Serbian Chemical Society |
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| Online Access: | http://www.doiserbia.nb.rs/img/doi/0352-5139/2003/0352-51390305243N.pdf |
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doaj-af95c6e965874856996d0b169e3850792020-12-24T12:11:01ZengSerbian Chemical Society Journal of the Serbian Chemical Society0352-51391820-74212003-01-01684-524324810.2298/JSC0305243N0352-51390305243NChemical modification of β-lactoglobulin by quininesNovaković Irena0Vujčić Zoran M.1Božić Tatjana T.2Božić Nataša M.3Milosavić Nenad B.4Sladić Dušan M.5Institute of Chemistry, Technology and Metallurgy, Department of Chemistry, Njegoševa 12, P. O. Box 473, 11001 BelgradeFaculty of Chemistry, University of Belgrade, Studentski trg 12-16, P. O. Box 158, 11001 Belgrade, Serbia and MontenegroFaculty of Chemistry, University of Belgrade, Studentski trg 12-16, P. O. Box 158, 11001 Belgrade, Serbia and MontenegroFaculty of Chemistry, University of Belgrade, Studentski trg 12-16, P. O. Box 158, 11001 Belgrade, Serbia and MontenegroFaculty of Chemistry, University of Belgrade, Studentski trg 12-16, P. O. Box 158, 11001 Belgrade, Serbia and MontenegroFaculty of Chemistry, University of Belgrade, Studentski trg 12-16, P. O. Box 158, 11001 Belgrade, Serbia and MontenegroThe 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.http://www.doiserbia.nb.rs/img/doi/0352-5139/2003/0352-51390305243N.pdfavaronequinoneβ-lactoglobulincovalent modification. |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Novaković Irena Vujčić Zoran M. Božić Tatjana T. Božić Nataša M. Milosavić Nenad B. Sladić Dušan M. |
| spellingShingle |
Novaković Irena Vujčić Zoran M. Božić Tatjana T. Božić Nataša M. Milosavić Nenad B. Sladić Dušan M. Chemical modification of β-lactoglobulin by quinines Journal of the Serbian Chemical Society avarone quinone β-lactoglobulin covalent modification. |
| author_facet |
Novaković Irena Vujčić Zoran M. Božić Tatjana T. Božić Nataša M. Milosavić Nenad B. Sladić Dušan M. |
| author_sort |
Novaković Irena |
| title |
Chemical modification of β-lactoglobulin by quinines |
| title_short |
Chemical modification of β-lactoglobulin by quinines |
| title_full |
Chemical modification of β-lactoglobulin by quinines |
| title_fullStr |
Chemical modification of β-lactoglobulin by quinines |
| title_full_unstemmed |
Chemical modification of β-lactoglobulin by quinines |
| title_sort |
chemical modification of β-lactoglobulin by quinines |
| publisher |
Serbian Chemical Society |
| series |
Journal of the Serbian Chemical Society |
| issn |
0352-5139 1820-7421 |
| publishDate |
2003-01-01 |
| description |
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. |
| topic |
avarone quinone β-lactoglobulin covalent modification. |
| url |
http://www.doiserbia.nb.rs/img/doi/0352-5139/2003/0352-51390305243N.pdf |
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