http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2006508062-A
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2317-50 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K16-04 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/B01D- http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-18 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-20 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-06 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-18 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-53 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-531 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-563 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-04 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-395 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-08 |
| filingDate | 2003-09-11-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2006-03-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-2006508062-A |
| titleOfInvention | Isolation of immunoglobulin molecules lacking inter-heavy chain disulfide bonds. |
| abstract | The present invention relates to a method for reliable and controllable separation of immunoglobulin half antibodies from intact immunoglobulin antibodies, while retaining biological activity, as well as purified immunoglobulin half antibody preparations and purified immunoglobulins. To complete antibody preparations. The dissociated half antibody can be separated from the intact antibody by chromatography. There are four known subclasses of IgG molecules: IgG 1 ; IgG 2 ; IgG 3 ; and IgG 4 . IgG 4 molecules differ from other IgG isotypes in that disulfide bonds that link two heavy chain subunits are not necessarily formed. Noncovalent interactions which settled heavy chain subunits due heterogeneity of IgG 4 molecules are not clear after gel filtration of the purified IgG 4 protein. However, when the purified IgG4 protein is separated under non-reducing conditions by denaturing polyacrylamide gel electrophoresis (SDS-PAGE), two different protein species—complete antibodies and “half antibodies” can be identified. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2022520972-A |
| priorityDate | 2002-09-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 148.