Journal of the Serbian Chemical Society 2004 Volume 69, Issue 11, Pages: 901-907
doi:10.2298/JSC0411901S
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Protein covalent modification of biologically active quinones

Sladić Dušan M., Novaković Irena, Vujčić Zoran M., Božić Tatjana T., Božić Nataša M., Milić Dragan, Šolaja Bogdan A., Gašić Miroslav J.

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.

Keywords: quinone, avarone, steroidal quinones, β-lactoglobulin, covalent modification

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