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dc.contributor.authorHummon, A. B.zh_CN
dc.contributor.authorHuang, H. Q.zh_CN
dc.contributor.authorKelley, W. P.zh_CN
dc.contributor.authorSweedler, J. V.zh_CN
dc.contributor.author黄河清zh_CN
dc.date.accessioned2013-12-12T02:24:50Z
dc.date.available2013-12-12T02:24:50Z
dc.date.issued2002zh_CN
dc.identifier.citationJournal of Neurochemistry,82(6):1398-1405zh_CN
dc.identifier.issn0022-3042zh_CN
dc.identifier.otherISI:000177790000009zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65953
dc.description.abstractNeuropeptides are a complex set of signaling molecules produced through enzymatic cleavages from longer prohormone sequences. The most common cleavage sites in prohormones are basic amino acid residues; however, processing is observed at non-basic sites. Cleavage at Leu-Leu sequences has been observed in three Aplysia californica prohormones. To further investigate this unusual event, native and non-native synthetic peptides containing Leu-Leu residues are incubated with homogenates of Aplysia californica ganglia and the resulting products monitored with MALDI MS. Cleavage near and between Leu-Leu residues is observed in the abdominal and buccal ganglia homogenates, confirming the presence of an unidentified peptidase. In addition, fractions from an HPLC separation of buccal ganglia homogenates also produce cleavages at Leu-Leu residues. Products resulting from cleavage at Leu-Leu sites are observed and are produced in larger amounts in acidic and neutral pH ranges, and cleavage is inhibited by the addition of EDTA, suggesting a metal is required for activity.zh_CN
dc.language.isoen_USzh_CN
dc.subjectleucine-leucine cleavageszh_CN
dc.subjectMALDI MSzh_CN
dc.subjectneuropeptideszh_CN
dc.subjectprohormone processingzh_CN
dc.titleA novel prohormone processing site in Aplysia californica: the Leu-Leu rulezh_CN
dc.typeArticlezh_CN


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