Abstract
Previously purified maize acetylcholinesterase (AChE) was 88kDa dimmers consisting of 42-44kDa polypeptides. The full-length cDNA is 1471 nucleotides encoding 394 amino acid residues. The maize AChE homologs were widely distributed in plants but not in animals. The homologs in monocot shared high homology (92-64%) with maize AChE, whereas dicot showed relatively low homology against maize AChE (57-53%). Thus, we presume that there is difference of the primary structure or enzymatic function between monocot and dicot. In this study, purified AChE from siratro was 125kDa trimmers consisting of 41-42kDa polypeptides. The full-length cDNA is 1441 nucleotides encoding 384 amino acid residues. The homolog against siratro AChE shared 90% identity with soybean, while maize AChE showed low homology (45%). From the results, the primary structure and subunit of siratro AChE were clearly different from maize AChE. Meanwhile, the enzymatic properties of siratro AChE was nearly similar that of maize AChE.
