http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2004053355-A1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P13-001 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N11-14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N11-18 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P13-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N11-14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N11-18 |
| filingDate | 2001-05-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5443c65c9a4369d834dacba63ca40a93 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_29688aed05a1a320ba57fa66a25bb0dd |
| publicationDate | 2004-03-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | US-2004053355-A1 |
| titleOfInvention | Modular approach to on-line synthesis, drug discovery and biochemical transformations using immobilized enzyme reactors |
| abstract | A coupled system using extremely different enzymes with incompatible cofactors and reaction conditions has been constructed using standard liquid chromatographic formats and open tubular formats. One of the significant aspects of the present invention lies in the development of the liquid chromatographic on-line enzyme cascade. This has been illustrated by the biosynthetic pathway involving dopamine beta-hydroxylase and phenylethanolamine N-methyltransferase which encompass the synthesis of the key neurotransmitters, norepinephrine and epinephrine. The results demonstrate for the first time the immobilization of dopamine beta-hydroxylase and phenylethanolamine N-methyltransferase. The IMERs are active and can be used in a liquid chromatographic format for qualitative and quantitative determinations. The IMER-HPLC system can be used to carry out standard Michaelis-Menten enzyme kinetic studies and to quantitatively determine enzyme kinetic constants, identify specific enzyme inhibitors, provide information regarding the mode of inhibition and the inhibitor constants (K i ). A second significant aspect of the present invention lies in the ability of the immobilized enzyme reactors to be used independently or as a combination, thus providing a unique opportunity to explore the interrelationships between these enzymes, to investigate the source of diseases and to design new drug entities for identified clinical syndromes. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-115161297-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-115286422-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-111979219-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-111676258-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2006226082-A1 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-10695744-B2 |
| priorityDate | 2000-05-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 831.