http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2001508647-A
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-96466 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K5-0827 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-573 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-42 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-37 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-34 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K5-097 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K5-08 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K5-093 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K5-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K5-087 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K5-083 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-573 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N11-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-37 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-34 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-48 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-42 |
| filingDate | 1997-11-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2001-07-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-2001508647-A |
| titleOfInvention | Hydrolase binding assay |
| abstract | (57) [Summary]nBinding assays for proteases and phosphatases that contain cysteine at the binding site or that contain cysteine as a structural component required for enzyme binding are disclosed. The sulfhydryl group of cysteine is the nucleophilic group for the mechanistic proteolytic and hydrolytic properties of the enzyme. Using the assay, the enzyme binding ability of the new unknown ligand and the mixed compound can be measured by competitively binding to a known enzyme binding substance, eg, a known enzyme inhibitor. By using a mutant form in which the natural or innate wild-type enzyme cysteine is replaced by serine or another amino acid, such as alanine, the problem of interference caused during the assay procedure by foreign oxidizing and alkylating agents is eliminated. You. Oxidation or alkylation of the sulfhydryl group -SH (or -S-) of cysteine causes interference, which adversely affects the binding capacity of the enzyme. More specifically, the present invention discloses assays for tyrosine phosphatases and cysteine proteases utilizing the Scintillation Proximity Assay (SPA) method, for example, cathepsins such as cathepsin K (O2) and capsase. An important application of this assay is the discovery of compounds for treating and studying diabetes, immunosuppression, cancer, Alzheimer's disease and osteoporosis and the like. A novel feature gained by the use of mutant enzymes is that they can be used in a wide variety of assays, such as conventional colorimetric, photometric, spectrophotometric, radioimmunoassays and ligand binding competition assays. It can be expanded. |
| priorityDate | 1996-11-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
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