Immobilization of ?-chymotrypsin to magnetic particles and their use for proteolytic cleavage of porcine pepsin A

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F09%3A10001360" target="_blank" >RIV/00216208:11310/09:10001360 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Immobilization of ?-chymotrypsin to magnetic particles and their use for proteolytic cleavage of porcine pepsin A

Original language description

?-Chymotrypsin was immobilized to ?CHO activated commercial magnetic particles via the protein free amino groups. Immobilized protease was used to study the phosphorylation degree of porcine pepsin A, as a model acidic protein and phosphoprotein. The proteolytic digest obtained using the prepared immobilized ?-chymotrypsin was separated using RP-HPLC and immobilized metal affinity chromatography (IMAC) with Fe(III) ions prior to MALDI-TOF analysis: the presence of phosphopeptide in porcine pepsin A wasshown.

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

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/LC06044" target="_blank" >LC06044: Center for Experimental Hematology</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2009

Confidentiality

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

Name of the periodical

Journal of molecular catalysis b-enzymatic

ISSN

1381-1177

e-ISSN

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Volume of the periodical

60

Issue of the periodical within the volume

1-2

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

7

Pages from-to

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UT code for WoS article

000267248700003

EID of the result in the Scopus database

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