Identification by 2D-page analysis of salt-stress induced proteins in radish (Raphanus sativus).
The response of Raphanus sativus to salinity has been investigated. Salt-responsive proteins were detected by comparative 2D-PAGE analysis. Three polypeptides of 22, 28 and 28.5 kDa were isolated and subjected to microsequencing. The P22 possesses homology with members of the Kunitz family of trypsin inhibitor; the P28.5 is homologous to ascorbate peroxidase of several plant species while P28 did not exhibit significant homology with sequences archived in available databases.
Lopez
F
F
Laboratoire de Biochimie et Physiologie Végétales, CNRS URA 573, ENSAM-INRA, Montpellier, France.
Vansuyt
G
G
Derancourt
J
J
Fourcroy
P
P
Casse-Delbart
F
F
D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000032:analysis*; D012462:Saline Solution, Hypertonic / Q000494:pharmacology*
D010940:Plant Proteins; D012462:Saline Solution, Hypertonic