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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_60da379fb33c192ef77f86a60c5ac029
classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-80
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-96466
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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-37
filingDate 1997-07-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_7599c175acc524e0e68a7b1545e873fe
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_9a256f6b3ee6068aaf1bd73952c83c5d
publicationDate 1998-01-22-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CA-2260766-A1
titleOfInvention Regulation of apoptosis and in vitro model for studies thereof
abstract A cell-free system based on the cytosol of normally growing cells, which reproduces measurable aspects of the apoptotic program, is provided. The apoptotic program is initiated by addition of dATP in the specific exemplification of the HeLa 100,000 x g supernatant. Fractionation of the cytosol yielded a 15 kDa protein, identified by absorption spectrum and protein sequence as cytochrome c, that is required for in vitro apoptosis. Elimination of cytochrome c from cytosol by immunodepletion or inclusion of sucrose to stabilize mitochondria during cytosol preparation, diminished the apoptotic activity. Addition of exogenous cytochrome c to cytochrome c-depleted extracts restored apoptotic activity. Cells undergoing apoptosis in vivo showed increased release of cytochrome c to their cytosol, suggesting that mitochondria may function in apoptosis by releasing cytochrome c.
priorityDate 1996-07-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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