The determination of activity of the enzyme Rubisco in cell extracts of the dinoflagellate alga Symbiodinium sp. by manganese chemiluminescence and its response to short-term thermal stress of the alga

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dc.contributor.author Lilley, RM
dc.contributor.author Ralph, PJ
dc.contributor.author Larkum, AWD
dc.date.accessioned 2011-02-07T06:21:16Z
dc.date.issued 2010-06
dc.identifier.citation Plant, Cell and Environment, 2010, 33 (6), pp. 995 - 1004
dc.identifier.issn 0140-7791
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/13391
dc.description.abstract The dinoflagellate alga Symbiodinium sp., living in symbiosis with corals, clams and other invertebrates, is a primary producer in coral reefs and other marine ecosystems. The function of the carbon-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) in dinoflagellates is difficult to study because its activity is rapidly lost after extraction from the cell. We report procedures for the extraction of Rubisco from Symbiodinium cells and for stable storage. We describe a continuous assay for Rubisco activity in these crude cell extracts using the Mn2+ chemiluminescence of Rubisco oxygenase. Chemiluminescence time courses exhibited initial transients resembling bacterial Form II Rubisco, followed by several minutes of linearly decreasing activity. The initial activity was determined from extrapolation of this linear section of the time course. The activity of fast-frozen cell extracts was stable at -80 °C and, after thawing and storage on ice, remained stable for up to 1 h before declining non-linearly. Crude cell extracts bound [14C] 2-carboxy-D-arabitinol 1,5-bisphosphate to a high molecular mass fraction separable by gel filtration chromatography. After pre-treatment of Symbiodinium cell cultures in darkness at temperatures above 30 °C, the extracted Rubisco activities decreased, with almost complete loss of activity above 36 °C. The implications for the sensitivity to elevated temperature of Symbiodinium photosynthesis are assessed. © 2010 Blackwell Publishing Ltd.
dc.language eng
dc.relation.isbasedon 10.1111/j.1365-3040.2010.02121.x
dc.title The determination of activity of the enzyme Rubisco in cell extracts of the dinoflagellate alga Symbiodinium sp. by manganese chemiluminescence and its response to short-term thermal stress of the alga
dc.type Journal Article
dc.parent Plant, Cell and Environment
dc.journal.volume 6
dc.journal.volume 33
dc.journal.number 6 en_US
dc.publocation United States en_US
dc.identifier.startpage 995 en_US
dc.identifier.endpage 1004 en_US
dc.cauo.name SCI.Environmental Sciences en_US
dc.conference Verified OK en_US
dc.for 0607 Plant Biology
dc.personcode 890085
dc.personcode 111269
dc.personcode 995493
dc.percentage 100 en_US
dc.classification.name Plant Biology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords Carbon fixation
dc.description.keywords Carboxylase
dc.description.keywords Hermatypic corals
dc.description.keywords Oxygenase
dc.description.keywords Photosynthesis
dc.description.keywords Stability
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - C3
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true
utslib.collection.history Closed (ID: 3)


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