http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-9218516-A1

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_588f4799eeda38576f3d4784cef85ded
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-46
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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
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filingDate 1992-04-10-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cd36f08691af9df14ce9b3a362c2d8ab
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_86ea2e2bd8c4b41baedd273d526bd7d0
publicationDate 1992-10-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber WO-9218516-A1
titleOfInvention Novel endopeptidase
abstract There is provided by the invention a novel composition comprising, in at least partially purified form, an endopeptidase endogenous to biological cells. The endopeptidase is characterized by having a molecular weight of about 110,000 daltons as measured by SDS PAGE; by being substantially insensitive to PMSF, TPCK, E-64, leupeptin, bacitracin, phosphoramidon and pepstatin; by being substantially inhibited by EDTA and 1,10-phenanthroline; and by being capable of cleaving peptide substrate comprising an alpha helical structural of at least about twelve to fourteen amino acids wherein said helix has a hydrophobic face and a hydrophilic face, said cleavage occurring amino terminal to a lysine or arginine residue on the hydrophilic face positioned within the context of at least four nonpolar amino acids substantially aligned along the hydrophobic face of the helix.
priorityDate 1991-04-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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Total number of triples: 456.