Purification and enzymatic characterization of tobacco leaf ?-N-acetylhexosaminidase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10286865" target="_blank" >RIV/00216208:11310/14:10286865 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.biochi.2014.09.006" target="_blank" >http://dx.doi.org/10.1016/j.biochi.2014.09.006</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.biochi.2014.09.006" target="_blank" >10.1016/j.biochi.2014.09.006</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Purification and enzymatic characterization of tobacco leaf ?-N-acetylhexosaminidase

Popis výsledku v původním jazyce

The kinetic properties of ?-N-acetylhexosaminidase purified from tobacco (Nicotiana tabacum L.) leaves have been investigated. In addition to chromogenic pNP derivates, N,N'-diacetylchitobiose and N,N',N"-triacetylchitotriose were also used as substratesof ?-N-acetylhexosaminidase. The highest reaction rate and the affinity for the substrate were observed for pNP-GlcNAc; however, an excess of this substrate inhibits the reaction. The reaction rate with pNP-GalNAc as the substrate was found to be about85% of that obtained with pNP-GlcNAc. The hydrolysis of acetylated chitooligomers by ?-N-acetylhexosaminidase followed by separation and quantification using capillary electrophoresis was slower compared to pNP-GlcNAc. The pH optimum of ?-N-acetylhexosaminidase for individual substrates was found at 4.3-5.0 and the temperature optimum was 50-55 oC. Gel permeation chromatography and red native electrophoresis determined the relative molecular weight as 280 000 and the isoelectric point as

Název v anglickém jazyce

Purification and enzymatic characterization of tobacco leaf ?-N-acetylhexosaminidase

Popis výsledku anglicky

The kinetic properties of ?-N-acetylhexosaminidase purified from tobacco (Nicotiana tabacum L.) leaves have been investigated. In addition to chromogenic pNP derivates, N,N'-diacetylchitobiose and N,N',N"-triacetylchitotriose were also used as substratesof ?-N-acetylhexosaminidase. The highest reaction rate and the affinity for the substrate were observed for pNP-GlcNAc; however, an excess of this substrate inhibits the reaction. The reaction rate with pNP-GalNAc as the substrate was found to be about85% of that obtained with pNP-GlcNAc. The hydrolysis of acetylated chitooligomers by ?-N-acetylhexosaminidase followed by separation and quantification using capillary electrophoresis was slower compared to pNP-GlcNAc. The pH optimum of ?-N-acetylhexosaminidase for individual substrates was found at 4.3-5.0 and the temperature optimum was 50-55 oC. Gel permeation chromatography and red native electrophoresis determined the relative molecular weight as 280 000 and the isoelectric point as

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/1M0505" target="_blank" >1M0505: Centrum cílených terapeutik</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Biochimie

ISSN

0300-9084

e-ISSN

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Svazek periodika

107 Part B

Číslo periodika v rámci svazku

December 2014

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

7

Strana od-do

263-269

Kód UT WoS článku

000347742400011

EID výsledku v databázi Scopus

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