| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a1dfd39878009ed672c93ba0247ee666 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A01K2217-05 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-43504 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-10
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-46
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-435
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-15
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-12
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A01K67-027
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A01K67-033
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A01H5-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C09K5-08
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-18 |
| filingDate |
2001-11-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate |
2004-06-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_9ad216eed156c3861216341ba7fc795e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cdcaaf92063035f7568be6ef536cd652
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_db40ce48826e722a6e6cd875093a5604
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_584f6aff39d6ed83478a6ad9804b4ed9 |
| publicationDate |
2004-06-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-6747130-B2 |
| titleOfInvention |
Tenebrio antifreeze proteins |
| abstract |
A novel class of thermal hysteresis (antifreeze) proteins (THP) that have up to 100 times the specific activity of fish antifreeze proteins has been isolated and purified from the mealworm beetle, Tenebrio molitor. Internal sequencing of the proteins, leading to cDNA cloning and production of the protein in bacteria has confirmed the identity and activity of the 8.4 to 10.7 kDa THP. They are novel Thr- and Cys-rich proteins composed largely of 12-amino-acid repeats of cys-thr-xaa-ser-xaa-xaa-cys-xaa-xaa-ala-xaa-thr. At a concentration of 55 mug/mL, the THP depressed the freezing point 1.6° C. below the melting point, and at a concentration of ~1 mg/mL the THP or its variants can account for the 5.5° C. of thermal hysteresis found in Tenebrio larvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-8734672-B2 |
| priorityDate |
1997-06-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |