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dc.contributor.authorCarraway, Robert E.
dc.contributor.authorCochrane, David E.
dc.contributor.authorRuane, Susan E.
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:44Z
dc.date.available2022-08-23T16:54:44Z
dc.date.issued1987-11-25
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1987 Nov 25;262(33):15886-9.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid2445741
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42569
dc.description.abstractTwo immunoreactive neurotensin-related peptides generated by the action of endogenous protease(s) on protein substrates during acid extraction of avian tissues have been isolated from extracts of turkey skin and proventriculus. One was identified as the pentadecapeptide, H-Phe-Glu-Arg-Phe-Gln-Gly-Met-Arg-Thy-Arg-Gly-Pro-Tyr-Phe-Leu-OH and the other was its C-terminal octapeptide fragment. Each peptide showed partial homology to the C-terminal, biologically active region of avian neurotensin, and isolated preparations displayed pharmacologic activity at submicromolar concentrations. Synthetic preparations were shown to be indistinguishable from the native peptides during high pressure liquid chromatography (HPLC) and bioassay. Analysis by HPLC indicated that similar peptides could be generated in extracts of proventriculus, pancreas, small intestine, skin, heart, lung, and skeletal muscle. These results, establishing the presence of a neurotensin-related sequence which can be liberated from protein(s) by the action of tissue enzyme(s), suggest that peptide(s) similar to neurotensin may be rapidly formed in order to promote physiologic regulation in multiple tissue(s).
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=2445741&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/262/33/15886.full.pdf+html
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectChickens
dc.subjectHistamine Release
dc.subjectHumans
dc.subjectKinetics
dc.subjectMast Cells
dc.subjectMolecular Sequence Data
dc.subjectNeurotensin
dc.subjectpurification
dc.subjectRats
dc.subjectSkin
dc.subjectSpecies Specificity
dc.subjectTurkeys
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleIsolation, structures, and biologic activity of neurotensin-related peptides generated in extracts of avian tissue
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume262
dc.source.issue33
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/905
dc.identifier.contextkey579794
html.description.abstract<p>Two immunoreactive neurotensin-related peptides generated by the action of endogenous protease(s) on protein substrates during acid extraction of avian tissues have been isolated from extracts of turkey skin and proventriculus. One was identified as the pentadecapeptide, H-Phe-Glu-Arg-Phe-Gln-Gly-Met-Arg-Thy-Arg-Gly-Pro-Tyr-Phe-Leu-OH and the other was its C-terminal octapeptide fragment. Each peptide showed partial homology to the C-terminal, biologically active region of avian neurotensin, and isolated preparations displayed pharmacologic activity at submicromolar concentrations. Synthetic preparations were shown to be indistinguishable from the native peptides during high pressure liquid chromatography (HPLC) and bioassay. Analysis by HPLC indicated that similar peptides could be generated in extracts of proventriculus, pancreas, small intestine, skin, heart, lung, and skeletal muscle. These results, establishing the presence of a neurotensin-related sequence which can be liberated from protein(s) by the action of tissue enzyme(s), suggest that peptide(s) similar to neurotensin may be rapidly formed in order to promote physiologic regulation in multiple tissue(s).</p>
dc.identifier.submissionpathoapubs/905
dc.contributor.departmentDepartment of Physiology
dc.source.pages15886-9


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