Solubilization of the plastidial lysophosphatidylcholine acyltransferase from Allium porrum leaves: towards plants devoid of eukaryotic plastid lipids?
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.
Akermoun
M
M
Laboratoire de Biogenèse Membranaire, UMR-CNRS 5544/ESTBB, Université V. Segalen-Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France.
Testet
E
E
Cassagne
C
C
Bessoule
J J
JJ
D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000490:Allium / Q000201:enzymology*; D002793:Cholic Acids; D003902:Detergents; D018515:Plant Leaves / Q000201:enzymology; D030821:Plants, Genetically Modified / Q000201:enzymology; D018087:Plastids / Q000201:enzymology*; D012995:Solubility
D002793:Cholic Acids; D003902:Detergents; D008243:1-Acylglycerophosphocholine O-Acyltransferase; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate