Scm. Kwok et al., MOLECULAR-CLONING AND SEQUENCE-ANALYSIS OF THE CDNA-ENCODING PORCINE ACROSIN INHIBITOR, DNA and cell biology, 13(4), 1994, pp. 389-394
A full-length cDNA encoding the porcine acrosin inhibitor has been iso
lated from a boar seminal vesicle cDNA library. Nucleotide sequence an
alysis of the 667-bp cDNA predicts a precursor protein of 97 amino aci
d residues, which includes a 26-residue signal peptide and a 71-residu
e secreted protein. The predicted amino acid sequence of the mature pr
otein agrees completely with that of the sperm-associated acrosin inhi
bitor determined by conventional amino acid sequence analysis. However
, the asparagine/aspartic acid and glutamine/glutamic acid substitutio
ns, as reported in the seminal plasma counterpart, have not been obser
ved. Southern blot analysis shows only a single hybridizing band with
three different restriction endonucleases, suggesting the presence of
a single copy of the acrosin inhibitor gene in the porcine genome.