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1 August 2011 Characterization of Phenoloxidase from the Bay Scallop Argopecten irradians
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Abstract

Phenoloxidase (PO) is one of the most important factors in the bivalve immune defense system. In the current study, the PO of the scallop Argopecten irradians was purified from hemocytes using linear-gradient native PAGE combined with catechol and Coomassie brilliant blue staining. The results show that purified PO had a molecular mass of 555 kDa in native PAGE and 55 kDa in denatured PAGE. The analysis of the kinetics indicated that the Km values of PO for L-DOPA, catechol, and hydroquinone were 0.51 mM/L, 0.23 mM/L, and 0.87 mM/L, respectively, which suggests that the PO was a type of p-diphenoloxidase. The PO had optimal activities at 40°C and a pH of 8.0, and its activity was greatly enhanced by Ca2 and Mg2 , and inhibited by Fe2 and Mn2 . In addition, the PO activity was inhibited by sodium sulfite, ascorbic acid, sodium diethyldithiocarbamate (DETC), cysteine, citric acid, and ethylenediamine tetraacetic acid disodium (EDTA). However, no inhibition was found when thiourea and sodium azide were used. Based on the inhibition that was induced by EDTA and DETC, we conclude that the PO of A. irradians was a copper-containing metalloenzyme.

Jingwei Jiang, Jing Xing, Xiuzhen Sheng, and Wenbin Zhan "Characterization of Phenoloxidase from the Bay Scallop Argopecten irradians," Journal of Shellfish Research 30(2), 273-277, (1 August 2011). https://doi.org/10.2983/035.030.0212
Published: 1 August 2011
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