Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris.

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris.

Original language description

The primary structure and proteolytic processing of the &#945;-amylase isoinhibitor &#945; AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of &#945;AI-1 was screened with a panel of the digestive &#945;-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 &#945;-amylases from three orders of insect (Coleoptera, Hymenoptera and Diptera) and an inhibition of &#945;-amylases of the annelid worm. The inhibitory potential of &#945;AI-1 against several &#945;-amylases was found to be modulated by pH. To understand how &#945;AI-1 discriminates among closely related &#945;-amylases, the sequences of the &#945;-amylases sensitive, respectively, insensitive to &#945;AI-1 were compared, and the critical determinants were localized on the spatial &#94

Czech name

Inhibitory spec. a insektic. selektivity na ;-amylase inhibitor z rostlin Phaseolus vulgaris

Czech description

The primary structure and proteolytic processing of the &#945;-amylase isoinhibitor &#945; AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of &#945;AI-1 was screened with a panel of the digestive &#945;-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 &#945;-amylases from three orders of insect (Coleoptera, Hymenoptera and Diptera) and an inhibition of &#945;-amylases of the annelid worm. The inhibitory potential of &#945;AI-1 against several &#945;-amylases was found to be modulated by pH. To understand how &#945;AI-1 discriminates among closely related &#945;-amylases, the sequences of the &#945;-amylases sensitive, respectively, insensitive to &#945;AI-1 were compared, and the critical determinants were localized on the spatial &#94

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

GF - Diseases, pests, weeds and plant protection

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2004

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Phytochemistry

ISSN

0031-9422

e-ISSN

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Volume of the periodical

66

Issue of the periodical within the volume

1

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

9

Pages from-to

31-39

UT code for WoS article

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EID of the result in the Scopus database

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