Abstract
Guinea pig prostate contains one major soluble esteropeptidase activity. The protein has been purified and characterized and found to be a glycoprotein comprised of a single polypeptide chain. The molecular has a similar Km for lysine and arginine synthetic substrates, although the Vmax for arginine is much greater than that for lysine. Amino-terminal sequence analysis has also revealed a marked degree of homology to mouse gamma-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to gamma-NGF, however, the guinea pig enzyme does not appear to form stable complexes with beta-NGF.
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