Proenkephalin A and proopiomelanocortin peptides in human cerebrospinal fluid.
作者： Danxia Liu , George W. Wood , Dominic M. Desiderio
DOI: 10.1016/S0378-4347(00)82328-2
关键词:
摘要: Precursors to beta-endorphin (BE) and methionine enkephalin (ME), proteolytic enzymes that cleave those BE ME precursors ME, were determined in several milliliters of human cerebrospinal fluid. Endogenous peptides purified by reversed-phase high-performance liquid chromatography (HPLC), detected with radioreceptor assay (RRA), radioimmunoassay, mass spectrometry (MS). Total opioid receptor activity measurements the profile HPLC-receptor CSF samples both used monitor neuropeptide metabolism. MS data linked molecular ion a unique fragment ion. A later-eluting fraction (84 min) 90-min HPLC gradient appeared all HPLC-RRA profiles, contained displaced [3H]etorphine, quantitative qualitative patterns profiles changed within few minutes elapsed between acquiring first second fluid samples. That 84-min was fractionated further more shallow 120-min into three sections displayed delta-opioid receptor-preferring activity, using [3H]ME as ligand. These hydrolyzed separately source for endogenous neuropeptides yield products correlated immunoreactive section I III.
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