Peptidases of pinworms Syphacia muris and Passalurus ambiguus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60460709%3A41210%2F10%3A22298" target="_blank" >RIV/60460709:41210/10:22298 - isvavai.cz</a>

Alternative codes found

RIV/67985823:_____/10:00355841

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Peptidases of pinworms Syphacia muris and Passalurus ambiguus

Original language description

In this first report about pinworms peptidases we primarily characterize peptidases released during in vitro maintenance of two common pinworms of laboratory animals - Syphacia muris and Passalurus ambiguus. The peptidase activity obtained using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed the presence of peptidases from S. muris with a wide range of molecular size (25-110 kDa), which degrades gelatin and mucin at alkaline pH levels. P. ambiguus released serine and aspartyl peptidases degrading gelatin at all tested pH (3, 5, 7, and 9) and at acidic pH Passalurus released aspartyl and cysteine peptidases which are active against mucin. (C) 2010 Elsevier Inc. All rights reserved.

Czech name

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Czech description

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Type

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

CEP classification

GJ - Diseases and animal vermin, veterinary medicine

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2010

Confidentiality

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

Name of the periodical

Experimental Parasitology

ISSN

0014-4894

e-ISSN

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Volume of the periodical

126

Issue of the periodical within the volume

2

Country of publishing house

US - UNITED STATES

Number of pages

5

Pages from-to

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UT code for WoS article

000280885500007

EID of the result in the Scopus database

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