Cyclic AMP affinity purification and ESI-QTOF MS-MS identification of cytosolic glyceraldehyde 3-phosphate dehydrogenase and two nucleoside diphosphate kinase isoforms from tobacco BY-2 cells.
FEBS Lett
; 508(1): 75-9, 2001 Nov 09.
Article
em En
| MEDLINE
| ID: mdl-11707271
ABSTRACT
The soluble protein fraction of tobacco bright yellow 2 cells contained adenosine 3',5'-cyclic monophosphate (cAMP)-binding activity, detected with both a conventional binding assay and a surface plasmon resonance biosensor. A cAMP-agarose-based affinity purification procedure yielded three proteins which were identified by mass spectrometry as glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and two nucleoside diphosphate kinases (NDPKs). This is the first report describing an interaction between cAMP and these proteins in higher plants. Our findings are discussed in view of the reported role of the interaction of cAMP with GAPDH and NDPK in animals and yeast. In addition, we provide a rapid method to isolate both proteins from higher plants.
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Base de dados:
MEDLINE
Assunto principal:
Nicotiana
/
AMP Cíclico
/
Núcleosídeo-Difosfato Quinase
/
Gliceraldeído-3-Fosfato Desidrogenases
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article