title: Identification by 2D-page analysis of salt-stress induced proteins in radish (Raphanus sativus).
abstract: 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.
authors.affiliation: Laboratoire de Biochimie et Physiologie Végétales, CNRS URA 573, ENSAM-INRA, Montpellier, France.
authors.forename: F
authors.initials: F
authors.lastname: Lopez
authors.forename: G
authors.initials: G
authors.lastname: Vansuyt
authors.forename: J
authors.initials: J
authors.lastname: Derancourt
authors.forename: P
authors.initials: P
authors.lastname: Fourcroy
authors.forename: F
authors.initials: F
authors.lastname: Casse-Delbart
mesh_terms: 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*
chemical_list: D010940:Plant Proteins; D012462:Saline Solution, Hypertonic