Purification of glyoxysomal acetyl-CoA acyltransferase.
Acetyl-CoA acyltransferase was extracted from cotyledons of germinating cucumber seeds and purified to apparent heomogeneity. The purification based primarily on cation exchange chromatography and separation on an affinity gel. The enzyme is a dimer consisting of two subunits of molecular weight 45 000. Acetyl-CoA acyltransferase was localized in glyoxysomes, the matrix was found to be the site of thiolase function within the organelle.
D000102:Acetyl-CoA C-Acyltransferase / Q000302:isolation & purification*; D000217:Acyltransferases / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008970:Molecular Weight; D009940:Organoids / Q000201:enzymology*; D010944:Plants / Q000201:enzymology*
D046911:Macromolecular Substances; D000217:Acyltransferases; D000102:Acetyl-CoA C-Acyltransferase