| dc.contributor.author |
Dimou, M |
en |
| dc.contributor.author |
Paunescu, A |
en |
| dc.contributor.author |
Aivalakis, G |
en |
| dc.contributor.author |
Flemetakis, E |
en |
| dc.contributor.author |
Katinakis, P |
en |
| dc.date.accessioned |
2014-06-06T06:49:17Z |
|
| dc.date.available |
2014-06-06T06:49:17Z |
|
| dc.date.issued |
2009 |
en |
| dc.identifier.issn |
14220067 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.3390/ijms10072896 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4508 |
|
| dc.subject |
Carbonic anhydrase |
en |
| dc.subject |
Glycine max |
en |
| dc.subject |
Hypocotyl |
en |
| dc.subject |
In situ hybridization |
en |
| dc.subject |
Phosphoenolpyruvate carboxylase |
en |
| dc.subject |
Pyruvate kinase |
en |
| dc.subject |
Root |
en |
| dc.subject.other |
carbon dioxide |
en |
| dc.subject.other |
carbonate dehydratase |
en |
| dc.subject.other |
digoxigenin |
en |
| dc.subject.other |
phosphoenolpyruvate carboxylase |
en |
| dc.subject.other |
plant extract |
en |
| dc.subject.other |
pyruvate kinase |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
cell division |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
gene expression |
en |
| dc.subject.other |
genetic transcription |
en |
| dc.subject.other |
histochemistry |
en |
| dc.subject.other |
human |
en |
| dc.subject.other |
immunolocalization |
en |
| dc.subject.other |
in situ hybridization |
en |
| dc.subject.other |
plant growth |
en |
| dc.subject.other |
plant metabolism |
en |
| dc.subject.other |
protein analysis |
en |
| dc.subject.other |
real time polymerase chain reaction |
en |
| dc.subject.other |
soybean |
en |
| dc.subject.other |
Western blotting |
en |
| dc.subject.other |
carbonic anhydrase |
en |
| dc.subject.other |
Glycine max |
en |
| dc.subject.other |
hypocotyl |
en |
| dc.subject.other |
in situ hybridization |
en |
| dc.subject.other |
phosphoenolpyruvate carboxylase |
en |
| dc.subject.other |
pyruvate kinase |
en |
| dc.subject.other |
root |
en |
| dc.subject.other |
Carbonic Anhydrases |
en |
| dc.subject.other |
Hypocotyl |
en |
| dc.subject.other |
Phosphoenolpyruvate Carboxylase |
en |
| dc.subject.other |
Plant Proteins |
en |
| dc.subject.other |
Plant Roots |
en |
| dc.subject.other |
Pyruvate Kinase |
en |
| dc.subject.other |
Soybeans |
en |
| dc.subject.other |
Glycine max |
en |
| dc.title |
Co-localization of carbonic anhydrase and phosphoenolpyruvate carboxylase and localization of pyruvate kinase in roots and hypocotyls of etiolated Glycine max seedlings |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.3390/ijms10072896 |
en |
| heal.publicationDate |
2009 |
en |
| heal.abstract |
We investigated the presence of carbonic anhydrase in root and hypocotyl of etiolated soybean using enzymatic, histochemical, immunohistochemical and in situ hybridization approaches. In parallel, we used in situ hybridization and immunolocalization to determine the expression pattern and localization of phosphoenolpyruvate carboxylase. Their co-localization in the root tip as well as in the central cylinder, suggests that a large fraction of the CO2 may be re-introduced into C4 compounds. GmPK3 expression, coding for a cytoplasmic isoform of pyruvate kinase, was detected in all different root cell types, suggesting that both phosphoenolpyruvate-utilizing enzymes are involved in phosphoenolpyruvate metabolism in etiolated soybean roots; a case indicative of the necessary flexibility plant metabolism has to adopt in order to compensate various physiological conditions. © 2009 by the authors; licensee Molecular Diversity Preservation International. |
en |
| heal.journalName |
International Journal of Molecular Sciences |
en |
| dc.identifier.issue |
7 |
en |
| dc.identifier.volume |
10 |
en |
| dc.identifier.doi |
10.3390/ijms10072896 |
en |
| dc.identifier.spage |
2896 |
en |
| dc.identifier.epage |
2910 |
en |