Purification of Glyoxysomal Acetyl-CoA Acyltransferase

Abstract
Acetyl-CoA acyltransferase was extracted from cotyledons of germinating cucumber [Cucumis sativus] seeds and purified to apparent homogeneity. The purification was based primarily on cation exchange chromatography and separation on an affinity gel. The enzyme is a dimer consisting of 2 subunits of MW 45,000. Acetyl-CoA acyltransferase was localized in glyoxysomes, the matrix being the site of thiolase function within the organelle.

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