http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-0068695-A2
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_46f8cf263e27134018abc1983cfd08f6 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-6833 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-68 |
| filingDate | 2000-05-12-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_de3757843c026e3e6bc0afd3d4da8853 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_672076c2144078a7afbd652b75676b08 |
| publicationDate | 2000-11-16-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | WO-0068695-A2 |
| titleOfInvention | Reagent and process for peptide/protein differentiation using circular dichroism detection |
| abstract | A reagent comprised of an aqueous solution of Cu(II)-D-histidine complex acts effectively as a devitalizing agent required to qualitatively identify an enantiomer and quantitatively determine its enantiomeric purities. The initial function of the host ligand (D-histidine) is to keep the Cu(II) ion in solution in high ph values. The base line CD spectrum associated with each Cu-(chiral ligand) host complex is uniquely different. On adding peptide or protein, exchange occurs between the host ligand (D-histidine) in the analyte ligand (protein). Exchanges produce changes in the CD spectrum that are significant enough that they have the potential of becoming a reliable spectroscopic fingerprint for every individual analyte. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-8664177-B2 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-9062093-B2 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-102034931-B http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-6939683-B2 |
| priorityDate | 1999-05-12-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 240.