| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_7776b07827d0789ab50c9a87a64a91aa
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_45475bb45af6588b5c8ac59dfff27874
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a40c4afda2ae6c4f81a4dfc38bfb288d
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_bc5256be365101d0394467d78ffce395
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_2d175e87b542837089a64bcda8c60574 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-904 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-54
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-32
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y101-9901
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-006
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0006 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-32
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-54
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-04 |
| filingDate |
2012-06-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate |
2015-07-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_04d2da244bde1e3c06aca66888accff3
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_738fdc3fb462aff797a21a9fbf17b3e7
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_202609362cedb95074bd8d47abd22abd
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f7670fe63305c194116094ec65d742ef |
| publicationDate |
2015-07-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-9074239-B2 |
| titleOfInvention |
Flavin-binding glucose dehydrogenase, method for producing flavin-binding glucose dehydrogenase, and glucose measurement method |
| abstract |
A flavin-binding glucose dehydrogenase (FAD-GDH), which in addition to having high substrate specificity and adequate desirable heat stability, is suitable for efficient production, preferably using E. coli , yeast or molds and the like as host cells. The FAD-GDH has amino acid substitutions at positions equivalent to one or more locations selected from the group consisting of position 213, position 368 and position 526 in the amino acid sequence described in SEQ ID NO: 8. The FAD-GDH is acquired from a culture by inserting a gene encoding the FAD-GDH into host cells such as E. coli . A preferable example of the FAD-GDH is FAD-GDH, in which a signal peptide region present in an N-terminal region has been deleted from the amino acid sequence of Mucor-derived FAD-GDH, and which has the aforementioned amino acid substitutions. The FAD-GDH can be preferably used in clinical diagnosis. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-10490837-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2014057331-A1
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/EP-4067483-A1
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-9238802-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-9493814-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-9469844-B2 |
| priorityDate |
2011-06-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |