PURIFICATION AND PROPERTIES OF A 35 KDA GLYCOPROTEIN FROM SPERMATHECAL EXTRACT OF EYPREPOCNEMIS-PLORANS (INSECTA, ORTHOPTERA) WITH AXONEMALCYTOSKELETON DISASSEMBLY ACTIVITY

A glycoprotein (gp35) was purified from spermathecal extract of the or thopteran Eyprepocnemis plorans by FPLC gel filtration. Using an in vi tro assay, this protein was found to be the only spermathecal extract component capable of inducing modifications of the sperm flagellum sim ilar to those observed in vivo. This biological activity is achieved d uring the course of sexual maturation. Intact gp35 migrated in SDS-PAG E as a doublet with 34 and 36 kDa components, becoming a single band a fter complete deglycosylation. The protein also has a unique N-terminu s. Chemical deglycosylation revealed that the carbohydrate component a ccounts for about 10% of the total protein mass. Its pi was found to b e slightly acidic. Radiolabeled gp35 bound the sperm surface with typi cal receptor-ligand kinetics. Copyright (C) 1996 Elsevier Science Ltd.