About: Facile production of Aspergillus niger a-N-acetylgalactosaminidase in yeast

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	a-N-Acetylgalactosaminidase (a-GalNAc-ase; EC.3.2.1.49) is an exoglycosidase specific for the hydrolysis of terminal a-linked N-acetylgalactosamine in various sugar chains. The cDNA corresponding to the a-GalNAc-ase gene was cloned from Aspergillus niger, sequenced, and expressed in the yeast Saccharomyces cerevisiae. The a-GalNAc-ase gene contains an open reading frame which encodes a protein of 487 amino acid residues. The molecular mass of the mature protein deduced from the amino acid sequence of this reading frame is 54 kDa. The recombinant protein was purified to apparent homogeneity and biochemically characterized (pI 4.4, KM 0.56 mmol/l for 2-nitrophenyl 2-acetamido-2-deoxy-a-D-galactopyranoside, and optimum enzyme activity was achieved at pH 2.0-2.4 and 50-55 _C). Its molecular weight was determined by analytical ultracentrifuge measurement and dynamic light scattering. Our experiments confirmed that the recombinant a-GalNAc-ase exists as two distinct species (70 and 130 kDa) compared to its native form, which is purely monomeric. N-Glycosylation was confirmed at six of the eight potential N-glycosylation sites in both wild type and recombinant a-GalNAc-ase. a-N-Acetylgalactosaminidase (a-GalNAc-ase; EC.3.2.1.49) is an exoglycosidase specific for the hydrolysis of terminal a-linked N-acetylgalactosamine in various sugar chains. The cDNA corresponding to the a-GalNAc-ase gene was cloned from Aspergillus niger, sequenced, and expressed in the yeast Saccharomyces cerevisiae. The a-GalNAc-ase gene contains an open reading frame which encodes a protein of 487 amino acid residues. The molecular mass of the mature protein deduced from the amino acid sequence of this reading frame is 54 kDa. The recombinant protein was purified to apparent homogeneity and biochemically characterized (pI 4.4, KM 0.56 mmol/l for 2-nitrophenyl 2-acetamido-2-deoxy-a-D-galactopyranoside, and optimum enzyme activity was achieved at pH 2.0-2.4 and 50-55 _C). Its molecular weight was determined by analytical ultracentrifuge measurement and dynamic light scattering. Our experiments confirmed that the recombinant a-GalNAc-ase exists as two distinct species (70 and 130 kDa) compared to its native form, which is purely monomeric. N-Glycosylation was confirmed at six of the eight potential N-glycosylation sites in both wild type and recombinant a-GalNAc-ase. (en)
Title	Facile production of Aspergillus niger a-N-acetylgalactosaminidase in yeast Facile production of Aspergillus niger a-N-acetylgalactosaminidase in yeast (en)
skos:prefLabel	Facile production of Aspergillus niger a-N-acetylgalactosaminidase in yeast Facile production of Aspergillus niger a-N-acetylgalactosaminidase in yeast (en)
skos:notation	RIV/00216208:11310/12:10104139!RIV13-GA0-11310___
http://linked.open...avai/predkladatel	Přírodovědecká fakulta
http://linked.open...avai/riv/aktivita	I P S Z
http://linked.open...avai/riv/aktivity	I, P(1M0505), P(GA303/09/0477), P(GAP207/10/0321), P(GD305/09/H008), S, Z(AV0Z50200510), Z(MSM0021620808)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Weignerová, Lenka Bezouška, Karel Vaněk, Ondřej Mrázek, Hynek
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	Univerzita Karlova v Praze / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	136013
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/12:10104139
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Glycosylation analysis; Glycosidase; Expression; a-N-Acetylgalactosaminidase; Aspergillus niger (en)
http://linked.open.../riv/klicoveSlovo	Aspergillus niger Glycosidase Expression Glycosylation analysis a-N-Acetylgalactosaminidase
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[045F8E4ED8D8]
http://linked.open...i/riv/nazevZdroje	Protein Expression and Purification
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Center of targeted therapeutic drugs Preparation, biotransformation, and optimalization of compounds with antitumor and antimicrobial effects Glycomic and proteomic analysis of the molecular mechanisms of elimination of clinically relevant tumors by killer cells of the immune system The ways to N-acetyl-mannosamine structures via mannoside metabolizing enzymes
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	81
http://linked.open...iv/tvurceVysledku	Benada, Oldřich Bezouška, Karel Křen, Vladimír Man, Petr Vaněk, Ondřej Weignerová, Lenka Mrázek, Hynek
http://linked.open...ain/vavai/riv/wos	000297438800017
http://linked.open...n/vavai/riv/zamer	Microorganisms in Research and Biotechnology Molekulárně biologické, genetické a epigenetické aspekty vzniku a rozvoje modelových tumorů dospělého věku. Význam pro epidemiologii, časnou diagnostiku a léčbu
issn	1046-5928
number of pages	9 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.pep.2011.09.009
http://localhost/t...ganizacniJednotka	11310
is http://linked.open...avai/riv/vysledek of	Facile production of Aspergillus niger a-N-acetylgalactosaminidase in yeast

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