http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2001169779-A
Outgoing Links
Predicate | Object |
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assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_aa908c0be49131bbf813d5a8635918ff http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_77eb3729063c124de4dc853b66b966f1 |
classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-645 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-48 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-14 |
filingDate | 1999-12-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c6080278557c0d407b3884dc091f6df4 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_74e229a905a3f76f313f4a10e99252a6 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_ef7a5edbeb644c28d56eb8021a40f58d http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b1d854a40086f285834d99d0cfb637b6 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b23bf5278b385a173f79c0ec7ffb4bad |
publicationDate | 2001-06-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | JP-2001169779-A |
titleOfInvention | Aminopeptidase and method for producing the same |
abstract | (57) [Summary] (Modified)nPROBLEM TO BE SOLVED: To provide a product derived from maitake, which has been difficult to separate and purify. Enzymatic properties, genetic information of aminopeptidase and its Providing efficient manufacturing methods.nSOLUTION: It is derived from Maitake and has the following properties: Aminopeptidase and a method for producing the same.n(A) optimum pH and stable pH range: optimum pH is 8.5, pH is low in the range of 6.0 to 10.5 (45 ° C, 1 hour) Fixed.n(B) Optimum temperature: The optimum temperature is 65 ° C.n(C) Thermal stability: stable at 55 ° C. or less.n(D) Substrate specificity: Leucine and phenylalanine for.n(E) Molecular weight: The molecular weight is 30 kDa (SDS-Polyac Lilamide gel electrophoresis).n(F) Effect of inhibitor: EDTA and phenanthroline More inactivated, inhibited by bestatin.n(G) Effect of metal ions: The enzyme inactivated by EDTA Mn 2+ , Zn 2+ , Cu 2+ And Co 2+ Active by addition of Conversion.n(H) N-terminal amino acid sequence: specific sequence. |
priorityDate | 1999-12-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 107.