Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F09%3A00010321" target="_blank" >RIV/61989592:15310/09:00010321 - isvavai.cz</a>

Alternative codes found

RIV/60162694:G44__/09:00002182

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

Original language description

AA prolyl endoprotease from Aspergillus niger was isolated from the commercial product Brewers Clarex to evaluate itspossible application in proteomics. A colorimetric assessment with phenol and sulfuric acid showed the presence of neutral sugars (9 % ofweight). The subsequent treatment with N-glycosidase F released a variety of high-mannose type N-glycans, which were successfully detected using MALDI-TOF MS.MALDI-TOF/TOF tandem MS analysis of glycopeptides from a tryptic digest of prolyl endoproteaseunraveled the identity of the N-glycosylation site in the primary structure. Spectrophotometric measurements demonstrated optimal activity at pH 4.0-4.5 and also high thermostability for the cleavage at the C-terminal part of proline residues. The enzymeacts upon proline and alanine residues, but there is an additional minor cleavage at some other residues. The digestion of a honeybee peptide comprising six proline residues (apidaecin 1A) led to the detection of specific peptides termin

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

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Publication year

2009

Confidentiality

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

Name of the periodical

Journal of Mass Spectrometry

ISSN

1076-5174

e-ISSN

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Volume of the periodical

44

Issue of the periodical within the volume

11

Country of publishing house

DE - GERMANY

Number of pages

9

Pages from-to

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UT code for WoS article

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EID of the result in the Scopus database

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