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1.
Prikl Biokhim Mikrobiol ; 44(1): 101-5, 2008.
Artigo em Russo | MEDLINE | ID: mdl-18491605

RESUMO

We studied the effect of two proteins, PSPI-21 and PKSI, on the growth and development of phytopathogenic microorganisms (Phytophthora infestans oomycete and Fusarium culmorum fungus). Both proteins were isolated from potato tubers (Solanum tuberosum L., cv. Istrinskii) and served as inhibitors of serine proteinases. These proteins differed in the ability to inhibit growth of Phytophthora infestans oomycete and Fusarium culmorum fungus. PSPI-21 was the most potent in modulating the growth of oomycete mycelium. PKSI primarily affected the growth of the fungal mycelium. The proteins under study induced complete destruction of oomycete zoospores and partial destruction of fungal macroconidia. Our results suggest that these proteins are involved in the protection of potato plants from phytopathogenic microorganisms.


Assuntos
Fusarium/efeitos dos fármacos , Phytophthora/efeitos dos fármacos , Proteínas de Plantas/farmacologia , Inibidores de Serina Proteinase/farmacologia , Solanum tuberosum/química , Fusarium/crescimento & desenvolvimento , Peptídeos e Proteínas de Sinalização Intracelular/farmacologia , Micélio/efeitos dos fármacos , Micélio/crescimento & desenvolvimento , Fosfoproteínas/farmacologia , Phytophthora/crescimento & desenvolvimento , Tubérculos/química , Inibidores de Serina Proteinase/isolamento & purificação
2.
Biokhimiia ; 60(11): 1844-52, 1995 Nov.
Artigo em Russo | MEDLINE | ID: mdl-8590757

RESUMO

A novel trypsin and chymotrypsin inhibitor has been isolated from potato (Solanum tuberosum L.) tubers. The isolation procedure included ammonium sulfate precipitation, gel-chromatography on Sephadex G-75 and ion-exchange chromatography on DEAE-cellulose. The inhibitor interacts with trypsin and chymotrypsin at a molar ratio of 1:1. The substrate-dependent dissociation of the enzyme-inhibitor complexes is observed. The inhibitor displays no activity towards subtilisin and pancreatic elastase. The ability of the inhibitor to form a ternary complex containing simultaneously both trypsin and chymotrypsin molecules testifies to the presence of two independent reactive sites for these enzymes.


Assuntos
Quimotripsina/antagonistas & inibidores , Inibidores da Tripsina/isolamento & purificação , Sequência de Aminoácidos , Cromatografia DEAE-Celulose , Cromatografia em Gel , Eletroforese em Gel de Poliacrilamida , Dados de Sequência Molecular , Especificidade por Substrato , Inibidores da Tripsina/metabolismo
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