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A Basic 18-Amino Acid Peptide Contains the Polysulfate-Binding Domain Responsible for Activation of the Boar Proacrosin/Acrosin System¹

^a Laboratory of Embryology, Faculty of Biological Sciences, Pontifical Catholic University of Chile, Santiago, Chile

Proacrosin is the zymogen of acrosin, a serine protease localized in the acrosomal matrix of mammalian sperm. Proacrosin/acrosin binds to solubilized zona pellucida glycoproteins (ZPGs) and various polysulfates in a non-enzymatic mechanism. In addition, both polysulfates and ZPGs induce proacrosin activation once they bind to the polysulfate-binding domain (PSBD) of the enzyme. We show here that the peptide ⁴³IFMYHNNRRYHTCGGILL⁶⁰ inhibited the proacrosin activation induced by either fucoidan or ZPGs. In addition, the peptide was recognized by the monoclonal antibody C5F10, which is directed against the PSBD region. Our data suggest that the PSBD is composed of many "subsites" that may or may not interact with each other.

First decision: 3 December 1999.

¹ This work was supported by grant 1971234 from the Chilean Research Council (FONDECYT) to C.B. and grants from TWAS 96-089 and from PLACIR PLI 291/97 to R.D.M. R.D.M. was a recipient of a postdoctoral fellowship from the Pontifical Catholic University of Chile, grant RF 94025 15.

² Correspondence: Claudio Barros, Laboratory of Embryology, Portugal 35, 5th floor, Santiago, Chile. FAX: 56 2 222 5515; cbarros{at}genes.bio.puc.cl

³ Current address: Oregon Regional Primate Research Center, 505 NW 185th Ave., Beaverton, OR 97006.

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