THE STRUCTURES OF THE BOVINE AND PORCINE PROACROSIN GENES AND THEIR CONSERVATION AMONG MAMMALS

Sperm acrosin is a serine protease that is involved in the recognition , binding and penetration of the sperm of the zona pellucida of the ov um. The bovine and porcine genes were cloned and characterized. Alignm ent of the intron/exon structure of both genes with the previously cha racterized human, rat and mouse genes and with other serine protease g enes reveals that the coded sequence of the mammalian proacrosin is di stributed in 5 exons and the splice junction types are identical to th e exons encoding the catalytic domain of other serine protease genes, A comparison of the bovine, porcine, human, guinea pig, rabbit, rat an d mouse preproprotein sequences shows that the catalytic domain is hig hly conserved, while the sequence of the proline rich domain is very v ariable among the species, ranging from 28.9% to 68.8%.