Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-3-26
pubmed:abstractText
Cells permeabilized with chloroform yielded ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) activities nearly equal to those of cell extracts, thus indicating that both cytoplasmic and carboxysomal RuBisCO are functional in situ. The carboxysomal and cytoplasmic RuBisCO both form the CO2-Mg2(+)-enzyme ternary complex, as evidenced by stabilization with 2-C-carboxy-D-arabinitol-1,5-bisphosphate (CABP), a potent competitive inhibitor of RuBisCO. The data are consistent with the hypothesis that the carboxysome is functional in carbon dioxide fixation.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-13471458, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-199579, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-204219, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-2509426, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-2837891, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-3068183, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-4127632, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-4355679, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-4372937, http://linkedlifedata.com/resource/pubmed/commentcorrection/1995596-7356969
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
173
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1565-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
In situ assay of ribulose-1,5-bisphosphate carboxylase/oxygenase in Thiobacillus neapolitanus.
pubmed:affiliation
Department of Biological Sciences, Clemson University, South Carolina 29634.
pubmed:publicationType
Journal Article