http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-H0466085-A

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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-64
filingDate 1990-07-06-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1b0244a8675c25b16e789297c687107c
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publicationDate 1992-03-02-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-H0466085-A
titleOfInvention Prolyl endoperptidase and production thereof
abstract PURPOSE: To enable obtaining of a useful remedy, etc., by crushing human T cells or cultured cells thereof and fractionating cytoplasms. n CONSTITUTION: Human T cells are frozen and fused in a phosphoric acid buffer saline solution and then centrifuged at a high speed to provide a cytoplasmic fraction, which is then purified by high-performance liquid chromatography, etc., to produce the objective prolyl endopeptidase exhibiting the following physicochemical properties. Acting on peptides containing proline and specifically hydrolyzing peptide bonds on the carboxyl side of the proline. Substrate specificity; acting on synthetic substrates expressed by formula I (MCA is 4- methylcoumarinamide) and formula II without acting on synthetic substrates expressed by formulas III and IV (Bz is benzyl), formulas V and VI for other enzymes. Influence of pH; the maximum activity at about pH 6.2 and residual activity of ≥50% at pH 5-7.2. Influence of ions; deteriorating the activity in the presence of Cu +2 and Zn 2+ without deteriorating the activity in the presence of Mg 2+ , Mn 2+ , Ca 2+ and Co 2+ , exhibiting some deteriorating in activity in the presence of maleic acid, etc. Molecular weight; about 70K daltons (measured by a gel filtration method), etc. n COPYRIGHT: (C)1992,JPO&Japio
priorityDate 1990-07-06-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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