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pubmed-article:15760343pubmed:abstractTextWe investigated the enzymatic properties and immunohistochemical localization of cuticular hemocyanin, a known oxygen transporter in the prawn Penaeus japonicus. The molecular weight of hemocyanin purified from the cuticle was estimated to be 67-77 k using SDS-PAGE, and the purified protein was effectively converted into a phenoloxidase-like enzyme by an SDS-treatment. The activated enzyme catalyzed the o-hydroxylation of monophenols and the oxidation of o-diphenols and was inhibited by typical inhibitors of phenoloxidase. These characteristics were nearly identical to the enzymatic properties of hemolymph hemocyanin. Immunological detection showed a diffuse distribution of hemocyanin over the exocuticle and endocuticle, and a higher signal level was observed in the latter. Based on these results, roles of hemocyanin in various physiological processes such as immune response and sclerotization of the cuticle were discussed.lld:pubmed
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pubmed-article:15760343pubmed:authorpubmed-author:NishiokaTakaa...lld:pubmed
pubmed-article:15760343pubmed:authorpubmed-author:HirataTakashi...lld:pubmed
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pubmed-article:15760343pubmed:authorpubmed-author:AdachiKohsuke...lld:pubmed
pubmed-article:15760343pubmed:authorpubmed-author:EndoHirotoshi...lld:pubmed
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pubmed-article:15760343pubmed:pagination136-43lld:pubmed
pubmed-article:15760343pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15760343pubmed:year2005lld:pubmed
pubmed-article:15760343pubmed:articleTitleHemocyanin in the exoskeleton of crustaceans: enzymatic properties and immunolocalization.lld:pubmed
pubmed-article:15760343pubmed:affiliationDivision of Applied Biosciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.lld:pubmed
pubmed-article:15760343pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15760343pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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