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Phenoloxidase in the scallop Chlamys farreri: Purification and antibacterial activity of its reaction products generated in vitro
- Source :
-
Fish & Shellfish Immunology . Jan2012, Vol. 32 Issue 1, p89-93. 5p. - Publication Year :
- 2012
-
Abstract
- 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 10504648
- Volume :
- 32
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Fish & Shellfish Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 69842710
- Full Text :
- https://doi.org/10.1016/j.fsi.2011.10.025