Abstract
Purpose: In this study, we isolate, characterize, and identify the biochemical function of Aea-AGP-317 protein from male accessory gland of Aedes aegypti in order to find out what factors in the crude male accessory gland preparation possess apparent proteaselike function and how they are able to digest proteins such as glutathione S-transferase. Methods: Biochemical methods, including polyacrylamide gel electrophoresis, electroelution, N-terminal amino acid sequencing, polyclonal antibodies, and fractionation of the extract from male accessory glands, were used in an in vitro study to characterize the functional protein from male accessory gland of Ae. aegypti. Results: Aea-AGP-317 was able to digest denatured male accessory gland protein, denatured Aea-AGP-317 peptide. and Drosophila GST protein under 27℃. Conclusion: Our results suggest that under natural conditions Aea-AGP-317 peptide may increase mating success by removing or destroying the spermatozoa of previous mates.
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