dc.contributor.author |
Udagama-Randeniya, Preethi V. |
|
dc.contributor.author |
Savidge, Rodney A. |
|
dc.date.accessioned |
2021-05-23T12:39:52Z |
|
dc.date.available |
2021-05-23T12:39:52Z |
|
dc.date.issued |
1995 |
|
dc.identifier.citation |
37 |
en_US |
dc.identifier.other |
https://doi.org/10.1007/BF00192190 |
|
dc.identifier.uri |
http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5220 |
|
dc.description.abstract |
The 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.sponsorship |
This research was supported by Forestry Canada and the Natural Sciences and Engineering Research Council of Canada. |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Springer |
en_US |
dc.subject |
Pinus strobus L |
en_US |
dc.subject |
Cell wall |
en_US |
dc.subject |
Polyphenol oxidase |
en_US |
dc.subject |
Tracheid differentiation |
en_US |
dc.subject |
lignin |
en_US |
dc.subject |
Wood formation |
en_US |
dc.title |
Conifeiyl alcohol oxidase - a catechol oxidase? |
en_US |
dc.type |
Article |
en_US |