title: Phenoloxidase in the scallop Chlamys farreri: purification and antibacterial activity of its reaction products generated in vitro.
abstract: Phenoloxidase (PO) was purified from hemocytes of the scallop Chlamys farreri using native-PAGE and gel permeation column chromatography, and then substrate specificity and antibacterial activity generated from reaction products of purified PO were analyzed. The results showed purified PO had a molecular mass of 576 kDa in native-PAGE and 53 kDa in denatured PAGE, and could catalyze the substrates L-3,4-dihydroxyphenylalanine (L-DOPA), dopamine, catechol and hydroquinone suggesting it is a type of p-diphenoloxidase. Using dopamine as a substrate, PO reaction products significantly inhibited the growth of Vibrio alginolyticus, Vibrio parahaemolyticus and Aeromonas salmonicida. No significant inhibition was found in Streptococcus dysgalactiae, Streptococcus iniae, Micrococcus lysodeikticus and Edwardsiella tarda. When L-DOPA was used as a substrate, significant inhibition occurred in A. salmonicida only.
authors: Laboratory of Pathology and Immunology of Aquatic Animals, Ocean University of China, Qingdao 266003, China.
authors: Jing
authors: J
authors: Xing
authors: Jingwei
authors: J
authors: Jiang
authors: Wenbin
authors: W
authors: Zhan
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents; D001419:Bacteria / Q000187:drug effects*; D014442:Monophenol Monooxygenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology*; D049897:Pectinidae / Q000201:enzymology*; D013379:Substrate Specificity; D013997:Time Factors
chemical_list: D000900:Anti-Bacterial Agents; D014442:Monophenol Monooxygenase