http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-WO2012169512-A1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-904 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y101-9901 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0006 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-006 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-54 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-32 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-32 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-15 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-10 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-04 |
| filingDate | 2012-06-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2015-02-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-WO2012169512-A1 |
| titleOfInvention | Flavin-binding glucose dehydrogenase, method for producing flavin-binding glucose dehydrogenase, and method for measuring glucose using the same |
| abstract | Provided is a flavin-binding glucose dehydrogenase (FAD-GDH) having high substrate specificity and sufficient thermal stability, and preferably suitable for efficient production using Escherichia coli, yeast, mold, etc. as host cells. FAD-GDH having an amino acid substitution at a position corresponding to one or more of the group consisting of positions 213, 368 and 526 in the amino acid sequence set forth in SEQ ID NO: 8. A gene encoding this FAD-GDH is introduced into a host cell such as E. coli, and FAD-GDH is obtained from the culture. As a preferred example of the FAD-GDH of the present invention, FAD-GDH having the amino acid substitution described above, in which the signal peptide region present in the N-terminal region is deleted from the amino acid sequence of FAD-GDH derived from fungi. FAD-GDH having high substrate specificity and excellent thermal stability, which can be suitably used for clinical diagnosis and the like, can be produced efficiently. |
| priorityDate | 2011-06-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 191.