Detection of natural and induced phenoloxidase activities in human serum

Abstract Natural and induced phenoloxidase activities were detected in human serum using nine different phenolic substrates, namely, tyrosine, tyramine, L–DOPA, DL–DOPA, dopamine, catechol, hydroquinone, protocatechuic acid and pyrogallol. Phenoloxidase activity was induced anew in serum using exoge...

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Bibliographic Details
Published in:Human immunology 2012-10, Vol.73 (10), p.1005-1010
Main Authors: Manikandan, Beulaja, Ramar, Manikandan
Format: Article
Language:English
Subjects:
Allergy and Immunology
Detergents - pharmacology
Enzyme Induction
Humans
Hydroquinones - metabolism
Hydroquinones - pharmacology
Monophenol Monooxygenase - antagonists & inhibitors
Monophenol Monooxygenase - biosynthesis
Monophenol Monooxygenase - blood
Oxidation-Reduction
Peptide Hydrolases - pharmacology
Phenols - metabolism
Phenols - pharmacology
Polysorbates - pharmacology
Pronase - pharmacology
Sodium Dodecyl Sulfate - pharmacology
Substrate Specificity
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Summary:Abstract Natural and induced phenoloxidase activities were detected in human serum using nine different phenolic substrates, namely, tyrosine, tyramine, L–DOPA, DL–DOPA, dopamine, catechol, hydroquinone, protocatechuic acid and pyrogallol. Phenoloxidase activity was induced anew in serum using exogenous elicitors, such as proteases or detergents. Among the proteases and detergents tested, pronase, SDS and Tween 20 were the best elicitors of phenoloxidase activities in serum, wherein, hydroquinone was the best phenolic substrate for both untreated as well as pronase treated serum and SDS or Tween 20 treated serum resulted in highest oxidation of dopamine or tyrosine, respectively. In the present study, all these oxidative reactions were inhibited by phenoloxidase inhibitors, namely, PTU and tropolone, thereby, confirming the role of phenoloxidase in human serum.
ISSN:0198-8859
1879-1166
DOI:10.1016/j.humimm.2012.07.331