Magnetic Bead Cellulose as a Suitable Support for Immobilization of alpha-Chymotrypsin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F12%3A11462" target="_blank" >RIV/00216208:11110/12:11462 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61389013:_____/12:00382141 RIV/00216208:11310/12:10126758

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s12010-012-9772-y" target="_blank" >http://dx.doi.org/10.1007/s12010-012-9772-y</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Magnetic Bead Cellulose as a Suitable Support for Immobilization of alpha-Chymotrypsin

Popis výsledku v původním jazyce

Magnetic bead cellulose was prepared by a suspension method from the mixture of viscose and magnetite using thermal sol-gel transition and regeneration of cellulose. The prepared magnetic particles after their activation with divinyl sulfone were shown to be suitable magnetic carrier for immobilization of alpha-chymotrypsin and for its application in proteomic studies. The specific activity of the immobilized proteinase was high; its activity did not change in the course of storage. The following properties of the immobilized proteinase were compared with those of the soluble enzyme: pH and temperature dependence of the activity, self-cleavage activity, and possibility of repeated use. alpha-Chymotrypsin immobilized to magnetic bead cellulose was usedfor the proteolytic digestion of porcine pepsin A and human gastric juice and a possibility of direct use of enzyme reaction products for matrix-assisted laser desorption/ionization time of flight mass spectrometry analysis was shown.

Název v anglickém jazyce

Magnetic Bead Cellulose as a Suitable Support for Immobilization of alpha-Chymotrypsin

Popis výsledku anglicky

Magnetic bead cellulose was prepared by a suspension method from the mixture of viscose and magnetite using thermal sol-gel transition and regeneration of cellulose. The prepared magnetic particles after their activation with divinyl sulfone were shown to be suitable magnetic carrier for immobilization of alpha-chymotrypsin and for its application in proteomic studies. The specific activity of the immobilized proteinase was high; its activity did not change in the course of storage. The following properties of the immobilized proteinase were compared with those of the soluble enzyme: pH and temperature dependence of the activity, self-cleavage activity, and possibility of repeated use. alpha-Chymotrypsin immobilized to magnetic bead cellulose was usedfor the proteolytic digestion of porcine pepsin A and human gastric juice and a possibility of direct use of enzyme reaction products for matrix-assisted laser desorption/ionization time of flight mass spectrometry analysis was shown.

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

2012

Kód důvěrnosti údajů

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

Název periodika

Applied biochemistry and biotechnology

ISSN

0273-2289

e-ISSN

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Svazek periodika

168

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

295-305

Kód UT WoS článku

000309224300007

EID výsledku v databázi Scopus

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