Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027006%3A_____%2F10%3A00001292" target="_blank" >RIV/00027006:_____/10:00001292 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Popis výsledku v původním jazyce

Microplate assays with 96 wells were optimized to screen proteolytic activities in mite homogenates. Whole-mite extracts of seven species of mites exhibited non-specific proteolytic activity in buffers from pH 2 to 12, and three peaks of highest activityat pH 3, 5-6, and 10 were distinguished. The reducing agent Tris(2-carboxyethyl) phosphine hydrochloride decreased general proteolytic activity on azocasein at pH 5 and 6. The results obtained on two non-specific substrates, azocasein and azoalbumin, showed highly different ranks of the species at pH 5 and 6. Evidence of the presence of proteolytic activities on all tested substrates and in all the tested mite homogenates suggests that the proteolytic activities may contribute to allergenicity. Poor orundetected hydrolytic activities of mite extracts toward substrates for keratin and collagen at digestive pH underline the importance of ecological interactions between mites and microorganisms in the utilization of such substrates.

Název v anglickém jazyce

Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Popis výsledku anglicky

Microplate assays with 96 wells were optimized to screen proteolytic activities in mite homogenates. Whole-mite extracts of seven species of mites exhibited non-specific proteolytic activity in buffers from pH 2 to 12, and three peaks of highest activityat pH 3, 5-6, and 10 were distinguished. The reducing agent Tris(2-carboxyethyl) phosphine hydrochloride decreased general proteolytic activity on azocasein at pH 5 and 6. The results obtained on two non-specific substrates, azocasein and azoalbumin, showed highly different ranks of the species at pH 5 and 6. Evidence of the presence of proteolytic activities on all tested substrates and in all the tested mite homogenates suggests that the proteolytic activities may contribute to allergenicity. Poor orundetected hydrolytic activities of mite extracts toward substrates for keratin and collagen at digestive pH underline the importance of ecological interactions between mites and microorganisms in the utilization of such substrates.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Archives of Insect Biochemistry and Physiology

ISSN

0739-4462

e-ISSN

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Svazek periodika

75

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

20

Strana od-do

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Kód UT WoS článku

000283778200004

EID výsledku v databázi Scopus

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