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2.
Biochemistry (Mosc) ; 75(5): 590-7, 2010 May.
Artigo em Inglês | MEDLINE | ID: mdl-20632938

RESUMO

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.


Assuntos
Pisum sativum/metabolismo , Proteínas de Plantas/biossíntese , Proteoma/análise , Ácido Salicílico/farmacologia , Eletroforese em Gel Bidimensional , Pisum sativum/efeitos dos fármacos , Folhas de Planta/efeitos dos fármacos , Folhas de Planta/metabolismo , Proteômica , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
6.
Biochemistry (Mosc) ; 66(1): 68-71, 2001 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-11240395

RESUMO

All investigated exogenous phytohormones (jasmonic, salicylic, and abscisic acids) induced the appearance of (14)C-label in a polypeptide with molecular mass 29 kD that was not found in the control; these acids also increased [(14)C]leucine incorporation into a 25-kD polypeptide and decreased such incorporation into a 45-kD polypeptide. This can be considered as a nonspecific response of the plants to the action of these hormones. Salicylic and abscisic (but not jasmonic) acids induced the synthesis of a 19-kD polypeptide, and jasmonate induced the synthesis of a 96-kD polypeptide.


Assuntos
Ácido Abscísico/farmacologia , Ciclopentanos/farmacologia , Leucina/metabolismo , Folhas de Planta/metabolismo , Proteínas de Plantas/metabolismo , Ácido Salicílico/farmacologia , Radioisótopos de Carbono , Oxilipinas , Pisum sativum
7.
Biochemistry (Mosc) ; 64(7): 780-2, 1999 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-10424901

RESUMO

Chitinase and proteinase activities were found in aphroproteins excreted by larvae of the cicada Aphrophora costalis Mats; this accounts for their fungicidal effect. Aphroproteins did not show DNase or RNase activities and did not exhibit properties of proteinase inhibitors. The data suggest that larval foam protects the larva and host plant from entomogenous and phytopathogenic fungi.


Assuntos
Quitinases/metabolismo , Endopeptidases/metabolismo , Proteínas de Insetos/metabolismo , Serratia marcescens/enzimologia
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