Abstract
A gene encoding Drosophila melanogaster secretory phospholipase A2 (sPLA2) has been cloned and characterized(.) The coding region of the sPLA2 gene was interrupted by a short intron, and codes for a signal peptide of 18 amino acids, followed by a mature protein of 168 amino acids, containing the structural features of group III sPLA2. From a Northern blot analysis, about a 1.0-kb Drosophila sPLA2 transcript was found to be expressed throughout its development and in both the adult bodies and heads. The recombinant Drosophila sPLA2 expressed and purified in Escherichia coli was found to be Ca(+2)-dependent and maximally active at pH 5.
