Protein covalent modification of biologically active quinones

Autor: Sladić Dušan M., Novaković Irena, Vujčić Zoran M., Božić Tatjana T., Božić Nataša M., Milić Dragan, Šolaja Bogdan A., Gašić Miroslav J.
Jazyk: angličtina
Rok vydání: 2004
Předmět:
Zdroj: Journal of the Serbian Chemical Society, Vol 69, Iss 11, Pp 901-907 (2004)
Druh dokumentu: article
ISSN: 0352-5139
1820-7421
DOI: 10.2298/JSC0411901S
Popis: 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.
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