http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-H0994088-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_fd569fbfa1953ca9b7b375510e4d2763 |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-01 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-24 |
| filingDate | 1995-09-14^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_03a3b85354cd4eed283fe2cb0948fe42 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_343f55a104e53348656c123ca7af5daa http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e83df0a03d94deb03e8c133cd05f27d1 |
| publicationDate | 1997-04-08^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-H0994088-A |
| titleOfInvention | Novel glycopeptidase and method for producing the same |
| abstract | (57) Abstract: A glycopeptidase having an optimum pH around neutral pH and a method for producing the enzyme by a microorganism are provided. SOLUTION: Sphingobacteria mOL12- Bacteria belonging to the genus Sphingobacterium such as 4s are cultured, and glycopeptidase having the following properties is collected from the culture. Action: Hydrolyzes the bond between the asparagine residue and the N-acetylglucosamine residue in the glycoprotein or glycopeptide. Substrate specificity: It acts on a glycoprotein or glycopeptide containing an asparagine-linked sugar chain. Optimum reaction pH: stable at around pH 7 at 25 ° C. pH range: pH 5-9 at 25 ° C. Optimal reaction temperature: around 25 ° C. at pH 7.1 Thermal stability: Not deactivated for at least 48 hours at 25 ° C. |
| priorityDate | 1995-07-24^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Showing number of triples: 1 to 679 of 679.