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

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About: Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	An acidic prolyl endoprotease from Aspergillus niger was isolated from the commercial product Brewers Clarex (TM) to evaluate its possible application in proteomics. The chromatographic purification yielded a single protein band in sodium dodecyl sulfate polyacrylamide gel electrophoresis providing an apparent molecular mass of 63 kDa and a broad peak (mlz 58 061) in linear matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) indicating the glycoprotein nature of the enzyme. Indeed, a colorimetric assessment with phenol and sulfuric acid showed the presence of neutral sugars (9% of weight). 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 endoprotease unraveled the identity of the N-glycosylation site in the primary structure. The data obtained also show that the enzyme is presen An acidic prolyl endoprotease from Aspergillus niger was isolated from the commercial product Brewers Clarex (TM) to evaluate its possible application in proteomics. The chromatographic purification yielded a single protein band in sodium dodecyl sulfate polyacrylamide gel electrophoresis providing an apparent molecular mass of 63 kDa and a broad peak (mlz 58 061) in linear matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) indicating the glycoprotein nature of the enzyme. Indeed, a colorimetric assessment with phenol and sulfuric acid showed the presence of neutral sugars (9% of weight). 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 endoprotease unraveled the identity of the N-glycosylation site in the primary structure. The data obtained also show that the enzyme is presen (en)
Title	Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics (en)
skos:prefLabel	Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics (en)
skos:notation	RIV/60162694:G44__/09:00002182!RIV10-MO0-G44_____
http://linked.open...avai/riv/aktivita	S Z
http://linked.open...avai/riv/aktivity	S, Z(MO0FVZ0000501), Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika	44
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Řehulka, Pavel
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Ministerstvo obrany / Univerzita obrany - Fakulta vojenského zdravotnictví Hradec Králové
http://linked.open...dnocenehoVysledku	318356
http://linked.open...ai/riv/idVysledku	RIV/60162694:G44__/09:00002182
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Aspergillus niger; Brewers Clarex; digestion; glycan; MALDI-TOF; proline; prolyl endoprotease (en)
http://linked.open.../riv/klicoveSlovo	Aspergillus niger glycan MALDI-TOF proline digestion Brewers Clarex prolyl endoprotease
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[6D90EDB4210D]
http://linked.open...i/riv/nazevZdroje	Journal of Mass Spectrometry
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...UplatneniVysledku	2009
http://linked.open...v/svazekPeriodika	2009
http://linked.open...iv/tvurceVysledku	Šebela, Marek Řehulka, Pavel Chmelík, Josef Franc, Vojtěch Řehulková, Helena Raus, Martin Oždian, Tomáš Kábrt, Jaromír
http://linked.open...ain/vavai/riv/wos	000272150300006
http://linked.open...n/vavai/riv/zamer	Zdravotnická problematika ZHN Modulation of signalling and regulatory pathways in normal and cancer cells
issn	1076-5174
number of pages	9 (xsd:int)
http://localhost/t...ganizacniJednotka	G44
is http://linked.open...avai/riv/vysledek of	Identification of N-glycosylation in prolyl endoprotease from Aspergillus niger and evaluation of the enzyme for its possible application in proteomics

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