Laccase-1 in the pea aphid, Acyrthosiphon pisum (Harris)

dc.contributor.authorLiang, Qixin
dc.date.accessioned2006-06-26T14:52:14Z
dc.date.available2006-06-26T14:52:14Z
dc.date.graduationmonthAugust
dc.date.issued2006-06-21
dc.date.published2006
dc.description.abstractLaccases belong to the “multicopper oxidase” family of proteins, and can oxidize o-diphenols and p-diphenols in the presence of molecular oxygen. Laccases have been well characterized in wood-rotting fungi where they appear to play a role in lignin degradation, morphogenesis, and stress defense. More recently, laccase-2 has been found to play a role in the insect cuticle sclerotization and tanning. In addition, it has been hypothesized that laccase-1 may be involved in the oxidation of toxic phenolic compounds ingested by insects during feeding. A laccase-type phenoloxidase has been identified in the pea aphid, Acyrthosiphon pisum (Harris) using a combination of substrates that react with laccase. Within the pea aphid, laccase-1 transcript was found to be localized within the gut and the salivary glands. Finally, the specific regions where laccase-1 was present in the salivary gland was visualized using immunohistochemistry.
dc.description.advisorGerald R. Reeck
dc.description.degreeMaster of Science
dc.description.departmentBiochemistry
dc.description.levelMasters
dc.format.extent6849603 bytes
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/2097/172
dc.language.isoen_US
dc.publisherKansas State University
dc.rights© the author. This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.subjectLaccase
dc.subjectAphid
dc.subjectSalivary
dc.subjectphenoloxidase
dc.titleLaccase-1 in the pea aphid, Acyrthosiphon pisum (Harris)
dc.typeThesis

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