Enkephalinase: Selective inhibitors and partial characterization
dc.contributor.author | Sullivan, Sue | en_US |
dc.contributor.author | Akil, Huda | en_US |
dc.contributor.author | Blacker, Deborah | en_US |
dc.contributor.author | Barchas, Jack D. | en_US |
dc.date.accessioned | 2006-04-07T17:25:35Z | |
dc.date.available | 2006-04-07T17:25:35Z | |
dc.date.issued | 1980 | en_US |
dc.identifier.citation | Sullivan, Sue, Akil, Huda, Blacker, Deborah, Barchas, Jack D. (1980)."Enkephalinase: Selective inhibitors and partial characterization." Peptides 1(1): 31-35. <http://hdl.handle.net/2027.42/23269> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T0M-47STW1N-17/2/108ef51ee07c0137412315d656e40994 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23269 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6264406&dopt=citation | en_US |
dc.description.abstract | There are at least two types of enzymes in brain, endopeptidases and aminopeptidases, which metabolize enkephalins. Evidence is presented to suggest that enkephalinase, an endopeptidase cleaving at the Gly-Phe bond, is specific for the endogenous enkephalinergic system. Selective inhibitors are described for each enzyme. These are parachloromercuriphenylsulfonic acid and puromycin in the case of aminopeptidases and various enkephalin fragments in the case of enkephalinase. Some characteristics of the two types of enzymes are described. Enkephalinase has many properties in common with the well-characterized brain angiotensin-converting enzyme. These two enzymes, however, behaved differently when tested for chloride dependance, for activity in several buffers and for susceptibility to specific inhibitors. | en_US |
dc.format.extent | 449933 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 | Enkephalinase: Selective inhibitors and partial characterization | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Mental Health Research Institute, University of Michigan, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationother | Nancy Pritzker Laboratory of Behavioral Neurochemistry, Department of Psychiatry and Behavioral Sciences Stanford University School of Medicine, Stanford, CA 94305, USA | en_US |
dc.contributor.affiliationother | Nancy Pritzker Laboratory of Behavioral Neurochemistry, Department of Psychiatry and Behavioral Sciences Stanford University School of Medicine, Stanford, CA 94305, USA | en_US |
dc.contributor.affiliationother | Nancy Pritzker Laboratory of Behavioral Neurochemistry, Department of Psychiatry and Behavioral Sciences Stanford University School of Medicine, Stanford, CA 94305, USA | en_US |
dc.identifier.pmid | 6264406 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23269/1/0000206.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0196-9781(80)90032-7 | en_US |
dc.identifier.source | Peptides | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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