Facile production of Aspergillus niger ?-N-acetylgalactosaminidase in yeast
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00377419" target="_blank" >RIV/61388971:_____/12:00377419 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.pep.2011.09.009" target="_blank" >http://dx.doi.org/10.1016/j.pep.2011.09.009</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.pep.2011.09.009" target="_blank" >10.1016/j.pep.2011.09.009</a>
Alternative languages
Result language
angličtina
Original language name
Facile production of Aspergillus niger ?-N-acetylgalactosaminidase in yeast
Original language description
a-N-Acetylgalactosaminidase (a-GalNAc-ase; EC.3.2.1.49) is an exoglycosidase specific for the hydrolysis of terminal ?-linked N-acetylgalactosamine in various sugar chains. The cDNA corresponding to the ?-GalNAc-ase gene was cloned from Aspergillus niger, sequenced, and expressed in the yeast Saccharomyces cerevisiae. The ?-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-?-D-galactopyranoside, and optimum enzyme activity was achieved at pH 2.0?2.4 and 50?55oC). Its molecular weight was determined by analytical ultracentrifuge measurement and dynamic light scattering
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Expression and Purification
ISSN
1046-5928
e-ISSN
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Volume of the periodical
81
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
106-114
UT code for WoS article
000297438800017
EID of the result in the Scopus database
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