Solubilization of the plastidial lysophosphatidyfcholine acyltransferase from Allium porrum leaves: towards plants devoid of eukaryotic plastid lipids?. (December 2000)

• Record Type: Journal Article
• Authors: Akermoun, M.; Testet, E.; Cassagne, C.; Bessoule, J.-J.
• Is Part Of: Biochemical Society transactions. Volume 28:Number 6(2000)
• Page Start: 713
• Page End: 715
• Publication Date: 2000-12
• Subjects: CHAPS -- detergents -- phosphatidylcholine -- plastid envelope; lyso-PC, lysophosphatidyl-choline -- ER, endoplasmic reticulum; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0280713
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : To analyse the involvement of the plastidial lysophosphatidylcholine (lyso-PC) acyltransferase in the import of the extraplastidial lipid precursors required for eukaryotic plastid lipid synthesis, we plan to obtain transgenic plants. Since no sequence of lyso-PC acyltransferase is known, the purification of this enzyme has been undertaken to establish its sequence. First we determined the conditions allowing the solubilization of this membrane-bound enzyme. It is shown that by using CHAPS as a detergent, a lyso-PC acyltransferase activity is associated with the solubilized proteins.