Partial purification and characterization of a trypsin-like serine protease from bovine sperm

International Journal of Andrology
A CesariJorge Julián Sánchez

Abstract

Sperm proteolytic activities are relevant in the enzymatic mechanism of fertilization. Several authors have suggested the presence of serine proteases other than acrosin in mice and human spermatozoa. In this work we describe the characterization of a partially purified bovine sperm serine protease BSp66 and its dimmer, BSp120. Partial purification of the monomer was performed from fresh spermatozoa, while the dimer form of the protease was obtained from cryopreserved spermatozoa. The Mr of BSp120 and BSp66 estimated by zymography and gel filtration chromatography were 120 and 66 kDa, respectively. They were positively stained by Schiff-PAS reagent for glycoproteins and they both digested synthetic peptides with basic amino acids in the P1 site. Polyclonal antibodies against acrosin or proacrosin did not cross-react neither with BSp120, nor BSp66. In addition, antibodies raised in our laboratory against BSp120 and BSp66 did not recognize acrosin or proacrosin suggesting that they are not antigenically related proteins. Also, no cross- reactivity was detected with proteins in the range of 120-66 kDa when antibodies against the proteasome were used. The cellular localization of this protease by optical immunocytochemistry using s...Continue Reading

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Citations

Mar 8, 2005·Reproduction : the Official Journal of the Society for the Study of Fertility·A CesariM W Fornés
Jun 12, 2010·Theriogenology·Andreina CesariMiguel W Fornes
Oct 12, 2004·Biochemical and Biophysical Research Communications·A CesariM W Fornés
Oct 19, 2006·Insect Biochemistry and Molecular Biology·Susan J Davies, Tracey Chapman
Jun 12, 2013·Gene·Hai-Tao Mao, Wan-Xi Yang

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