Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50432
DC FieldValueLanguage
dc.contributor.authorLin, L.J.en_US
dc.contributor.author曾志正zh_TW
dc.contributor.authorLiao, P.C.en_US
dc.contributor.authorYang, H.H.en_US
dc.contributor.authorTzen, J.T.C.en_US
dc.date2005zh_TW
dc.date.accessioned2014-06-06T08:49:30Z-
dc.date.available2014-06-06T08:49:30Z-
dc.identifier.issn0981-9428zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/50432-
dc.description.abstractSeed oil bodies comprise a triacylglycerol matrix shielded by a monolayer of phospholipids and proteins. These surface proteins include an abundant structural protein, oleosin, and at least two minor protein classes termed caleosin and steroleosin. Two steroleosin isoforms (41 and 39 kDa), one caleosin (27 kDa), and two oleosin isoforms (17 and 15 kDa) have been identified in oil bodies isolated from sesame seeds. The signal peptides responsible for targeting of these proteins to oil bodies have not been experimentally determined. Hydropathy analyses indicate that the hydrophobic domain putatively responsible for oil-body anchoring is located in the N-terminal region of steroleosin, but in the central region of caleosin or oleosin. Direct amino acid sequencing showed that both steroleosin isoforms possessed a free methionine residue at their N-termini while caleosin and oleosin isoforms were N-terminally blocked. Mass spectrometry analyses revealed that N-termini of both caleosin and 17 kDa oleosin were acetylated after the removal of the first methionine. In addition, deamidation was observed at a glutamine residue in the N-terminal region of 17 kDa oleosin. (c) 2005 Elsevier SAS. All rights reserved.en_US
dc.language.isoen_USzh_TW
dc.relationPlant Physiology and Biochemistryen_US
dc.relation.ispartofseriesPlant Physiology and Biochemistry, Volume 43, Issue 8, Page(s) 770-776.en_US
dc.relation.urihttp://dx.doi.org/10.1016/j.plaphy.2005.07.008en_US
dc.subjectcaleosinen_US
dc.subjectN-terminal modificationen_US
dc.subjectoil-bodyen_US
dc.subjectoleosinen_US
dc.subjectsteroleosinen_US
dc.subjectsignal sequenceen_US
dc.subjectlipid bodiesen_US
dc.subjectin-vitroen_US
dc.subjectbiogenesisen_US
dc.subjectcellsen_US
dc.subjectseedsen_US
dc.subjectdehydrogenaseen_US
dc.subjectdeamidationen_US
dc.subjectacetylationen_US
dc.subjectexpressionen_US
dc.titleDetermination and analyses of the N-termini of oil-body proteins, steroleosin, caleosin and oleosinen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1016/j.plaphy.2005.07.008zh_TW
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextno fulltext-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.languageiso639-1en_US-
item.openairetypeJournal Article-
Appears in Collections:生物科技學研究所
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