Inhibitory spec. a insektic. selektivity na ;-amylase inhibitor z rostlin Phaseolus vulgaris
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60460709%3A41210%2F04%3A8184" target="_blank" >RIV/60460709:41210/04:8184 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris.
Popis výsledku v původním jazyce
The primary structure and proteolytic processing of the α-amylase isoinhibitor α AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of αAI-1 was screened with a panel of the digestive α-amylases from 30 species of insects, mites, gastropod, annelid worm, nematode and fungal phytopathogens with a focus on agricultural pests and important model species. This in vitro analysis showed a selective inhibition of α-amylases from three orders of insect (Coleoptera, Hymenoptera and Diptera) and an inhibition of α-amylases of the annelid worm. The inhibitory potential of αAI-1 against several α-amylases was found to be modulated by pH. To understand how αAI-1 discriminates among closely related α-amylases, the sequences of the α-amylases sensitive, respectively, insensitive to αAI-1 were compared, and the critical determinants were localized on the spatial ^
Název v anglickém jazyce
Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris.
Popis výsledku anglicky
The primary structure and proteolytic processing of the α-amylase isoinhibitor α AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of αAI-1 was screened with a panel of the digestive α-amylases from 30 species of insects, mites, gastropod, annelid worm, nematode and fungal phytopathogens with a focus on agricultural pests and important model species. This in vitro analysis showed a selective inhibition of α-amylases from three orders of insect (Coleoptera, Hymenoptera and Diptera) and an inhibition of α-amylases of the annelid worm. The inhibitory potential of αAI-1 against several α-amylases was found to be modulated by pH. To understand how αAI-1 discriminates among closely related α-amylases, the sequences of the α-amylases sensitive, respectively, insensitive to αAI-1 were compared, and the critical determinants were localized on the spatial ^
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
GF - Choroby, škůdci, plevely a ochrana rostlin
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2004
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Phytochemistry
ISSN
0031-9422
e-ISSN
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Svazek periodika
66
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
9
Strana od-do
31-39
Kód UT WoS článku
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EID výsledku v databázi Scopus
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