http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-104830891-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-84 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-81 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-46 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-18 |
| filingDate | 2015-03-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2017-10-31-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2017-10-31-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-104830891-B |
| titleOfInvention | A kind of Bungarus fasciatus antibacterial peptide Cath BF30 high efficiency preparation method |
| abstract | The invention discloses a kind of Bungarus fasciatus antibacterial peptide Cath BF30 high efficiency preparation method, step is as follows：Cath BF30 genes are designed and synthesized, its sequence is SEQ ID NO.1；Utilize Xho I with Xba I double digestions, pGAPZ α carriers are entered by the gene fragment clone of synthesis, obtain recombinant expression plasmid pGAPZ α Cath BF30；Recombinant expression plasmid is converted into Pichia pastoris, engineering bacteria SMD pGAPZ α 30 are obtained；Engineering bacteria is fermented under conditions of pH is less than 5；Fermentation supernatant is isolated and purified after 0.45 μm of membrane filtration removal of impurities using SP Sepharose FF posts.This method can realize efficient secretory expression, and ensure that secretory product has natural N end sequence, and secreting, expressing product has the activity for suppressing Propiobacterium, and fermentation supernatant only needs a step ion exchange to obtain high-purity C ath BF30. |
| priorityDate | 2015-03-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 46.