Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F12%3A00007377" target="_blank" >RIV/00023884:_____/12:00007377 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/1873-3468.12798" target="_blank" >http://dx.doi.org/10.1002/1873-3468.12798</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/1873-3468.12798" target="_blank" >10.1002/1873-3468.12798</a>

Result language
angličtina
Original language name
Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH
Original language description
Mouse acidic mammalian chitinase (AMCase) degrades chitin with highest efficiency at pH 2.0 and is active up to pH 8.0. Here, we report that mouse AMCase also exhibits transglycosylation activity under neutral conditions. We incubated natural and artificial chitin substrates with mouse AMCase at pH 2.0 or 7.0 and analyzed the resulting oligomers using an improved method of fluorescence assisted carbohydrate electrophoresis. Mouse AMCase produces primarily dimers of N-acetyl-D-glucosamine [(GlcNAc)2 ] under both pH conditions while generating transglycosylated (GlcNAc)3 primarily at pH 7.0 and at lower levels at pH 2.0. These results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs. This article is protected by copyright. All rights reserved.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30101 - Human genetics

Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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