http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-S5768785-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_6db78e3c1e9bf1b878d149a4db7c019d http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_b9822bceff022feda91b10019125e70f |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-50 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-48 |
| filingDate | 1980-10-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3c2a2cfeffc5e9175280a371306a65f2 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_879753f4f0871c91228326677b7989c0 |
| publicationDate | 1982-04-27-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-S5768785-A |
| titleOfInvention | Activity enhancement of protease |
| abstract | PURPOSE: To In cutting a peptide bond or carrying out a formation reaction using a metal protease, to enhance the activity of metal protease, by using methylamine or methylenediamin. n CONSTITUTION: For example, in forming amino acids shown by the formulasIand II by the formation of a peptide bond between the amino acid shown by the formula I(Z is benzyloxycarbonyl; Asp is aspartic acid residue) and the amino acid shown by the formula II(X is phenylalanine, tryprophan, tyrosine, leucine, isoleucine residue; R is lower alkyl or amino) or by the cutting of peptide bond shown by the formula III(Z, Asp, X, and R are as shown before) through an enzymatic reaction using a metal protease in an aqueous medium, about 0.5W2.5 mole methylamine or methylenediamine per l aqueous medium is added to the reaction system. n COPYRIGHT: (C)1982,JPO&Japio |
| priorityDate | 1980-10-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 27.