Please use this identifier to cite or link to this item: http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5220
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dc.contributor.authorUdagama-Randeniya, Preethi V.-
dc.contributor.authorSavidge, Rodney A.-
dc.date.accessioned2021-05-23T12:39:52Z-
dc.date.available2021-05-23T12:39:52Z-
dc.date.issued1995-
dc.identifier.citation37en_US
dc.identifier.otherhttps://doi.org/10.1007/BF00192190-
dc.identifier.urihttp://archive.cmb.ac.lk:8080/xmlui/handle/70130/5220-
dc.description.abstractThe physico-chemical properties of coniferyl alcohol oxidase (CAO), a copper containing glycoprotein spatiotemporally associated with lignification in conifers, is reported here. By electron paramagnetic resonance spectroscopy, only type 3 copper was indicated in CAO. CAO oxidizes several laccase substrates; however, it is not a blue-copper protein and monoclonal antibodies against both native and deglycosylated CAO did not recognize any of several laccases. The N-terminal sequence of CAO, H2N-X E L A Y S P P Y X P S, was non-homologous with known enzymes. Transparent copper, tetrameric structure, aminoacid composition, phenylhydrazine and tropolone inhibition, and SDS enhancement of CAO activity indicate that CAO is an o-diphenol oxidase.en_US
dc.description.sponsorshipThis research was supported by Forestry Canada and the Natural Sciences and Engineering Research Council of Canada.en_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.subjectPinus strobus Len_US
dc.subjectCell wallen_US
dc.subjectPolyphenol oxidaseen_US
dc.subjectTracheid differentiationen_US
dc.subjectligninen_US
dc.subjectWood formationen_US
dc.titleConifeiyl alcohol oxidase - a catechol oxidase?en_US
dc.typeArticleen_US
Appears in Collections:Department of Zoology

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