All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Direct comparison of chitinolytic properties and determination of combinatory effects of mouse chitotriosidase and acidic mammalian chitinase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F19%3A00008253" target="_blank" >RIV/00023884:_____/19:00008253 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0141813019318008" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813019318008</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ijbiomac2019.05.097" target="_blank" >10.1016/j.ijbiomac2019.05.097</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Direct comparison of chitinolytic properties and determination of combinatory effects of mouse chitotriosidase and acidic mammalian chitinase

  • Original language description

    Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been implicated in food processing and various pathophysiological conditions such as chronic inflammatory diseases. By combination of the colorimetric analysis and fluorophore-assisted carbohydrate electrophoresis (FACE) method, we directly compared the chitinolytic properties of mouse Chitl and AMCase and determined their combinatory effects in artificial and natural chitin substrates processing. Chitl and AMCase display different dynamics of chitinolytic properties through acidic to neutral conditions. At pH 2.0, the activity of AMCase was higher than that of Chitl and stronger or comparable with that of Serratia marcescens chitinase B, a well-characterized bacterium chitinase. Changes of degradation products using different substrates indicate that AMCase and Chitl have diverse properties under various pH conditions. Exposure of the chitin substrates to both Chit1 and AMCase did not indicate any mutual interference of these enzymes and showed no synergistic effect, in contrast to observations regarding some bacterial chitinases. Our results suggest that Chitl and AMCase have no synergistic effect under physiological conditions. (C) 2019 The Authors. Published by Elsevier B.V.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30101 - Human genetics

Result continuities

  • Project

  • Continuities

    N - Vyzkumna aktivita podporovana z neverejnych zdroju

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    International Journal Of Biological Macromolecules

  • ISSN

    0141-8130

  • e-ISSN

  • Volume of the periodical

    134

  • Issue of the periodical within the volume

    August

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    882-890

  • UT code for WoS article

    000474673600093

  • EID of the result in the Scopus database

    2-s2.0-85065870501