Proteomic analysis of salicylate-induced proteins of pea (Pisum sativum L.) leaves.
The effect of 50 microM salicylic acid on soluble proteins of pea (Pisum sativum L.) leaves was studied by proteomic analysis. Thirty-two salicylate-induced proteins were found, and 13 of these were identified using MALDI TOF MS. Salicylate-induced increased content was shown for the first time for the family 18 glycoside hydrolase, alpha-amylase, 33 kDa protein of photosystem II, lipid-desaturase-like protein, and glutamine amidotransferase. Increased content of protective proteins of direct antipathogenic action such as chitinase and beta-1,3-glucanases was also noted.
Tarchevsky
I A
IA
Kazan Institute of Biochemistry and Biophysics, Kazan Research Center, Russian Academy of Sciences, Kazan, 420111, Russia. tarchevsky@mail.knc.ru
Yakovleva
V G
VG
Egorova
A M
AM
D015180:Electrophoresis, Gel, Two-Dimensional; D018532:Pisum sativum / Q000187:drug effects / Q000378:metabolism*; D018515:Plant Leaves / Q000187:drug effects / Q000378:metabolism; D010940:Plant Proteins / Q000096:biosynthesis*; D020543:Proteome / Q000032:analysis*; D040901:Proteomics; D020156:Salicylic Acid / Q000494:pharmacology*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D010940:Plant Proteins; D020543:Proteome; D020156:Salicylic Acid