Rt. Richardson et Mg. Orand, CLONING AND SEQUENCING OF CDNAS FOR RABBIT PREPROACROSIN AND A NOVEL PREPROACROSIN-RELATED CDNA, Biochimica et biophysica acta, N. Gene structure and expression, 1219(1), 1994, pp. 215-218
A 1414 bp cDNA for rabbit preproacrosin (RPA) and a related short prep
roacrosin (shRPA) cDNA of 951 bp were cloned and sequenced. RPA's 431
amino acid open reading frame encodes a 46 422 kDa protein. shRPA is i
dentical to RPA except that it lacks an internal stretch of 468 bp, su
ch that the encoded protein has a deduced molecular mass of 29 965 kDa
. Antiserum against a synthetic peptide representing the light chain o
f rabbit proacrosin was used on Western blots of rabbit testis and spe
rm. Under reducing conditions, it revealed two major groups of bands a
t 50-57 and 29-32 kDa. Several lines of evidence suggest that shRPA is
a splice variant of proacrosin and that it encodes a 30-33 kDa protei
n similar to sperminogen (Siegel, M. et al. (1987) Biol. Reprod. 36, 1
063-1068), but apparently lacking proteinase activity.