A cDNA probe for recombinant human inhibin a subunit was used to scree
n an equine testis cDNA library. Approximately 220,000 plaques were sc
reened and 10 positive clones were identified. The largest of these cl
ones, approximately 1 kb, was sequenced. The sequence (993 nucleotides
[nt]) contained the ARG-ARG proteolytic processing site that precedes
the N-terminus of the a subunit mature peptide. The sequence that fol
lowed this processing site was 402 nt in length and encoded for a prot
ein of 134 amino acids. Nucleotide homology was 88%, 87%, 88%, 82% and
86% with the a subunit cDNA of cattle, pigs, sheep, mice and humans,
respectively. Amino acid homology within the mature peptide region was
99%, 88%, 92%, 87% and 86% with the a subunit of cattle, pigs, sheep,
mice and humans, respectively. The equine a subunit peptide contained
6 cysteine residues and one potential N-glycosylation site (Asn-Ile-S
er). The estimated molecular weight of the amino acid sequence for the
mature protein was 14.7 kDa. The equine inhibin a subunit cDNA was us
ed as a probe on a Northern blot of total RNA from various horse tissu
es. Positive hybridization (1.6 kb) was observed in the adrenal, corpo
ra lutea from mares 55 and 100 days pregnant, and testis RNA, but not
in the kidney, muscle, small intestine, liver from mares 55 and 100 da
ys pregnant, epididymis or lung.