Parallel inactivation of [alpha]2-adrenergic agonist binding and Ni by alkaline treatment
dc.contributor.author | Kim, Marian H. | en_US |
dc.contributor.author | Neubig, Richard R. | en_US |
dc.date.accessioned | 2006-04-07T18:54:10Z | |
dc.date.available | 2006-04-07T18:54:10Z | |
dc.date.issued | 1985-11-18 | en_US |
dc.identifier.citation | Kim, Marian H., Neubig, Richard R. (1985/11/18)."Parallel inactivation of [alpha]2-adrenergic agonist binding and Ni by alkaline treatment." FEBS Letters 192(2): 321-325. <http://hdl.handle.net/2027.42/25495> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T36-44KP5WW-75/2/357556d8fb79c9f94fdb7958a6560730 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/25495 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2998875&dopt=citation | en_US |
dc.description.abstract | [alpha]2-Adrenergic receptor-mediated inhibition of adenylate cyclase requires the guanine nucleotide-binding protein, Ni. This protein may also be required for stabilization of high-affinity [alpha]2-adrenergic agonist binding. Human platelet membranes treated under alkaline conditions (pH 11.5) exhibited a selective loss of high-affinity agonist binding as measured by P-[3H]aminoclonidine and [3H]UK 14,304. Binding of the antagonist [3H]yohimbine was largely unaffected with retention of> 60% of control binding sites. Ni determined by pertussis toxin-catalyzed [32P]ADP-ribosylation of cholate extracts from alkaline-treated membranes, was also markedly reduced. The parallel loss of of [alpha]2-agonist binding and Ni provides additional evidence that Ni, is required for [alpha]2-adrenergic agonist binding. | en_US |
dc.format.extent | 472089 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 | Parallel inactivation of [alpha]2-adrenergic agonist binding and Ni by alkaline treatment | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmacology, University of Michigan Medical School. Ann Arbor, MI 48109-0010, USA | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109-0010, USA; Department of Pharmacology, University of Michigan Medical School. Ann Arbor, MI 48109-0010, USA | en_US |
dc.identifier.pmid | 2998875 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/25495/1/0000036.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0014-5793(85)80134-4 | en_US |
dc.identifier.source | FEBS Letters | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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