Horseradish Peroxidase-Catalyzed Conjugation of Eugenol with Basic Amino Acids
作者:
MedeirosMarisa H. G.,
DimascioPaolo,
PintoAdriana P.,
VargasReinaldo R.,
BecharaEtelvino J. H.,
期刊:
Free Radical Research
(Taylor Available online 1996)
卷期:
Volume 25,
issue 1
页码: 5-12
ISSN:1071-5762
年代: 1996
DOI:10.3109/10715769609145651
出版商: Taylor&Francis
关键词: Eugenol;horseradish peroxidase;amino acids;eugenol-amino acid conjugation
数据来源: Taylor
摘要:
L-Lysine is shown to yield an adduct with the quinone methide intermediate formed during the horseradish peroxidase (HRP)-catalyzed aerobic oxidation of eugenol (4-allyl-2-methoxyphenol). Adduct formation is evidenced by (i) lysine quenching of the characteristic quinone methide absorption band measured at 350 ran; arginine and 7-aminobutyric acid, but not alanine or propionic acid showed similar behaviour (ii) lysine-promoted a 400 mV decrease of the eugenol oxidation voltammetric wave (1.00 V), concomitantly with an increase in current intensity and (iii) reverse phase HPLC isolation of the lysine eugenol adduct, followed by GC-MS analysis. The MS spectrum is consistent with a 2:1 lysineæugenol adduct (MW = 455). If operativein vivo, binding of lysine to eugenol might lead to protein inactivation and possibly be involved in eugenol toxicity.
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