Abstract
1. 1. Fatty acid synthetase from the insect C. capitata adults has been purified through homogeneity. 2. 2. Kinetic parameters as well as dependence of enzyme activity and stability on pH, temperature and ionic strength are studied. 3. 3. Molecular weight and amino acid composition of the protein as well as characterization of the lipid components associated with the protein are also reported. 4. 4. Comparison of the obtained results with those from the larval enzyme reveals some small differences between both enzymes, mainly related to ionic interactions maintaining the protein conformation and microenvironment of the aromatic residues, although they are not able to explain differences in terms of enzyme activity/enzyme content ratio during the development of the insect. Such differences are proposed to be related to the presence of some modulating agents.
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