Show simple item record

dc.contributor.supervisor Weselake, Randall
dc.contributor.supervisor Laroche, Andre
dc.contributor.author Foroud, Nora Afsaneh
dc.contributor.author University of Lethbridge. Faculty of Arts and Science
dc.date.accessioned 2007-05-17T14:48:47Z
dc.date.available 2007-05-17T14:48:47Z
dc.date.issued 2005
dc.identifier.uri https://hdl.handle.net/10133/256
dc.description xvii, 194 leaves ; 29 cm. en
dc.description.abstract Diacylglycerol acyltransferase (DGAT), an integral membrane protein of the endoplasmic reticulum, catalyses the final step in the sn-glycerol-3-phosphate pathway leading to triacylglycerol. Although DGAT has been cloned from a variety of species, including the major oilseed crop of Canada, canola (Brassica napus), little is known about the structure/function of the enzyme. BnDGAT1 is the major isoform of type I DGAT (DGAT-I) in microspore-derived cell suspension cultures of B. napus L. cv Jet Neuf, with the possible existence of a truncated form of BnDGAT1 known as BnDGAT2. In order to gain some insight into the topology of the enzyme, type I DGAT from B. napus was investigated using two approaches: (1) in vitro translation in the presence of microsomes and (2) immunochemical analyses of microsomes isolated from cell suspension cultures, both in combination with proteolytic mapping. Difficulties were encountered with the in vitro translation approach, possibly due to proper incorporation of the polypeptide into microsomal vesicles. Two cytocolic regions were identified in BnDGAT1, and one cytosolic region in putative BnDGAT2, using the immunochemical approach, thus providing some insight into the topology of B. napus DGAT-I. The results here support and nine and eight membrane-spanning topology for BnDGAT1 and BnGAT2, respectively. en
dc.language.iso en_US en
dc.publisher Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2005 en
dc.relation.ispartofseries Thesis (University of Lethbridge. Faculty of Arts and Science) en
dc.subject Dissertations, Academic en
dc.subject Membrane proteins en
dc.subject Diglycerides en
dc.subject Acyltransferases en
dc.subject Oilseed plants en
dc.subject Rape (Plant) -- Research en
dc.title Probing the membrane topology of a diacylglycerol acytransferase type I from Brassica Napus en
dc.type Thesis en
dc.publisher.faculty Arts and Science
dc.publisher.department Department of Chemistry and Biochemistry
dc.degree.level Masters


Files in this item

This item appears in the following Collection(s)

Show simple item record