http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-111499732-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_089d40759d5e23b2760341e8f5fd5ce8 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P7-08 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-805 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-805 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-16 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-42 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P7-08 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-34 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-113 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-107 |
| filingDate | 2020-04-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_24d0183f8ac9eda1e6924cf8092d42e9 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f03fd9f1c52c5e92313f90104fe075b2 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_6b4ca05845e3165bbb7b070f2c7d7f62 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_d6e2486edb1360733f7a1a175c8ca129 |
| publicationDate | 2020-08-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-111499732-A |
| titleOfInvention | A kind of hemoglobin oxygen carrier based on double chemical modification and its preparation method and application |
| abstract | The invention relates to a hemoglobin oxygen carrier based on double chemical modification, a preparation method and application thereof. In the hemoglobin oxygen carrier based on double chemical modification, two Val-1(α) residues are carboxymethylated, and two Lys The -99(α) residue is intramolecularly cross-linked. Two of the Lys-99(α) residues undergo intramolecular cross-linking, and the fumarimide bridge formed can change the electrostatic interaction of adult hemoglobin (HbA) molecules, stabilize the tonic state (T state) of HbA, and reduce its Oxygen affinity; Val-1(α) is located at the αα-terminal of the hole in the HbA center and can participate in the formation of salt bridges that help stabilize the relaxed state (R state) structure. The carboxylation modification will destroy these salt bridges and reduce HbA The stability of the R state makes the quaternary structure of HbA transfer from the R state to the T state, reducing the affinity of HbA for oxygen. The invention organically combines two modification means, improves the stability of HbA tetramer, enhances electrostatic interaction, improves the binding state of oxygen binding region and oxygen, and has strong oxygen carrying/releasing activity. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-112852772-A |
| priorityDate | 2020-04-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 68.