Human neutrophil phosphodiesterase
dc.contributor.author | Smolen, James E. | en_US |
dc.contributor.author | Geosits, Stephen J. | en_US |
dc.date.accessioned | 2006-09-11T14:56:46Z | |
dc.date.available | 2006-09-11T14:56:46Z | |
dc.date.issued | 1984-06 | en_US |
dc.identifier.citation | Smolen, James E.; Geosits, Stephen J.; (1984). "Human neutrophil phosphodiesterase." Inflammation 8(2): 193-199. <http://hdl.handle.net/2027.42/44535> | en_US |
dc.identifier.issn | 0360-3997 | en_US |
dc.identifier.issn | 1573-2576 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44535 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6086523&dopt=citation | en_US |
dc.description.abstract | Extracts of human neutrophils were examined for phosphodiesterase activity using a radiochemical assay. As reported by other investigators, both high- and low- K m forms of the enzyme were found. Although calmodulin could be measured in these extracts, human neutrophil phosphodiesterase proved not to be calmodulin dependent. Activity of the neutrophil phosphodiesterase was also not altered by physiologic concentrations of indomethacin, p -bromophenacyl bromide, eicosatetraenoic acid, or eicosatetraynoic acid, all inhibitors of arachidonic acid metabolism. These results are relevant to stimulus-secretion coupling in neutrophils, wherein calmodulin-dependent reactions play a vital role. | en_US |
dc.format.extent | 297147 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Medicine & Public Health | en_US |
dc.subject.other | Internal Medicine | en_US |
dc.subject.other | Rheumatology | en_US |
dc.subject.other | Pharmacology/Toxicology | en_US |
dc.subject.other | Pathology | en_US |
dc.title | Human neutrophil phosphodiesterase | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Pathology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Division of Rhematology, Department of Medicine, New York University School of Medicine, 10016, New York, New York; Division of Pediatric Hematology/Oncology, F6515 Mott Children's Hospital, University of Michigan Medical School, 48109, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationother | Division of Rhematology, Department of Medicine, New York University School of Medicine, 10016, New York, New York | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 6086523 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44535/1/10753_2004_Article_BF00916094.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF00916094 | en_US |
dc.identifier.source | Inflammation | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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