http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-101734863-B1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K1-14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K1-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N30-7233 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-6848 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N30-72 |
| filingDate | 2015-07-30-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2017-05-16-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2017-05-16-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | KR-101734863-B1 |
| titleOfInvention | Site-specific O-glycopeptide producing method and analytic method thereof |
| abstract | The present invention relates to a method for producing and analyzing a site-specific O-glycopeptide of a glycoprotein, and more specifically, a method for producing an O-glycopeptide using nonspecific proteolytic enzyme treatment, As well as an analytical method capable of quantitatively profiling the variability of the O-glycosides including the type of oligosaccharide bound to the site, the structure of the oligosaccharide variants and the oligosaccharide. The present invention has a shorter sample processing time than the conventional O-sugar diversity analysis method through β-elimination, and the produced O-glycopeptide has a short peptide length, which makes it easy to apply to a mass spectrometer. |
| priorityDate | 2015-07-30-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 82.