Properties of a CDP-Diglyceride Hydrolase from Guinea Pig Brain
dc.contributor.author | Rittenhouse, Harry G. | en_US |
dc.contributor.author | Seguin, Edward B. | en_US |
dc.contributor.author | Fisher, Stephen K. | en_US |
dc.contributor.author | Agranoff, Bernard W. | en_US |
dc.date.accessioned | 2010-04-01T14:56:57Z | |
dc.date.available | 2010-04-01T14:56:57Z | |
dc.date.issued | 1981-03 | en_US |
dc.identifier.citation | Rittenhouse, Harry G.; Seguin, Edward B.; Fisher, Stephen K.; Agranoff, Bernard W. (1981). "Properties of a CDP-Diglyceride Hydrolase from Guinea Pig Brain." Journal of Neurochemistry 36(3): 991-999. <http://hdl.handle.net/2027.42/65407> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/65407 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6110708&dopt=citation | en_US |
dc.description.abstract | Enzymatic hydrolysis of the pyrophosphate bond of CDP-diglyceride (CDP-DG), previously shown to occur in bacteria, is demonstrable in mammalian tissues. Activity was enriched in a lysosomal fraction obtained from guinea pig cerebral cortex and was purified 92-fold relative to the homogenate by a combination of XM-300 ultrafiltration and DEAE-cellulose column chromatography. When incubated with CDP-dipalmitin, the purified enzyme produced stoichiometric amounts of CMP and phosphatidate. dCDP-DG served as a substrate, while ADP-DG was an inhibitor, as were 5′-AMP and 5′-dAMP. CDP-DG hydrolysis was not affected by the presence of excess amounts of CDP-choline, CDP-glycerol, sodium pyrophosphate, or cyclic 3′,5′-AMP. | en_US |
dc.format.extent | 864206 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.rights | 1981 International Society for Neurochemistry Ltd. | en_US |
dc.subject.other | CDP-diglyceride Hydrolase | en_US |
dc.subject.other | Lysosomes | en_US |
dc.subject.other | Phosphatidate | en_US |
dc.subject.other | Cytidine 5′-Monophosphate | en_US |
dc.subject.other | Adenosine 5′-Monophosphate | en_US |
dc.title | Properties of a CDP-Diglyceride Hydrolase from Guinea Pig Brain | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Neuroscience Laboratory, Mental Health Research Institute and Department of Biological Chemistry, University of Michigan, 1103 E. Huron, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.identifier.pmid | 6110708 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/65407/1/j.1471-4159.1981.tb01691.x.pdf | |
dc.identifier.doi | 10.1111/j.1471-4159.1981.tb01691.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
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dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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