Abstract

Pigeon liver fatty acid synthetase multienzyme complex has been quantitatively dissociated in low ionic strength glycine-tris buffer into two subunits of identical or nearly identical molecular weight.A total of 5. 5 ± 1.0 readily titratable -SH groups/molecule are lost during the formation of the subunits. The dissociated enzyme is reconstituted to an active enzyme in high ionic strength buffer in the presence of dithiothreitol. The extent of reassociation is a function of the concentration of subunits. Under optimum conditions a complete recovery of enzyme activity is obtained.

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