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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_7f6e33603375c486b0ab3505830af9e8
classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-00
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-585
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-02
filingDate 1986-03-31-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_87df412580d987c0ebc989f36185c214
publicationDate 1987-02-07-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-S6229997-A
titleOfInvention Production of peptide having prolinamide at c terminal
abstract PURPOSE: To obtain the titled peptide efficiently and advantageously to cost, by reacting carboxypeptidase Y with a peptide having a specific amino acid in the presence of ammonia. n CONSTITUTION: Carboxypeptidase Y is reacted with a peptide having at least one amino acid selected from leucine, isoleucine, valine, phenylalanine and alanine at the C-terminal proline in the presence of ammonia. The amidation reaction for forming the peptide having the C-terminal prolinamide is carried out by mixing a previously prepared substrate solution with a carboxypeptidase solution and ammonia solution. Initially, the aqueous solution of the substrate is prepared. If the substrate is slightly soluble in water, the substrate can be dissolved in a 40% aqueous solution of dioxane. The aqueous solution of the carboxypeptidase Y enzyme specimen is then prepared. The amount of the carboxypeptidase Y to be used is such that 5μM final concentration based on 1mM substrate is obtained. n COPYRIGHT: (C)1987,JPO&Japio
priorityDate 1985-04-08-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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