Phosphatidate phosphatase : Activity and properties in fetal and adult rat lung
dc.contributor.author | Ravinuthala, H. Rao | en_US |
dc.contributor.author | Miller, Joseph C. | en_US |
dc.contributor.author | Weinhold, Paul A. | en_US |
dc.date.accessioned | 2006-04-07T16:58:59Z | |
dc.date.available | 2006-04-07T16:58:59Z | |
dc.date.issued | 1978-09-28 | en_US |
dc.identifier.citation | Ravinuthala, H. Rao, Miller, Joseph C., Weinhold, Paul A. (1978/09/28)."Phosphatidate phosphatase : Activity and properties in fetal and adult rat lung." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 530(3): 347-356. <http://hdl.handle.net/2027.42/22525> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1X-47F737R-133/2/1e22f8defd924daf0d8df27c8701d960 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22525 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=212108&dopt=citation | en_US |
dc.description.abstract | The purpose of this work is to compare the properties of phosphatidate phosphatase (-[alpha]-phosphatidate phosphohydrolase, EC 3.1.3.4) in fetal and adult rat lung and to establish the developmental profile of activity measured under optimal conditions. The maximal pH of 6.0-7.0 and the inhibition by fluoride, Ca2+ and detergents were similar for both adult and fetal. Phosphatidate phosphohydrolase activity was located in both mitochondria and microsomes. The localizations of marker enzymes indicated that the activity in these subfractions was not a result of cross contaminations. Very low activity was detected in the supernatant fraction and no Mg2+ requirement was demonstrable. The activity in the particulate fraction was about 50% of the adult from 18 day gestation until birth. Following birth, the activity rapidly increased to adult levels. Dipalmitoyl, dioleoyl and diacyl glycerol 3-phosphates are all utilized well as substrates. 1,2-dipalmitoyl-sn-glycerol 3-phosphate was hydrolyzed faster under maximal conditions. The velocity-substrate curves tended to be sigmoidal, particularly when 1,2-dipalmitoyl-sn-glycerol 3-phosphate was the substrate. Estimated apparent Km values of 0.02-0.03 mM were obtained for fetal and adult preparations. | en_US |
dc.format.extent | 803999 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Phosphatidate phosphatase : Activity and properties in fetal and adult rat lung | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Veterans Administration Hospital, and Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Veterans Administration Hospital, and Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Veterans Administration Hospital, and Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.identifier.pmid | 212108 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22525/1/0000069.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2760(78)90154-6 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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