| 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 weight of the deglycosylated protein is approximately 26,000. The esteropeptidase 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 γ-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to γ-NGF, however, the guinea pig enzyme does not appear to form stable complexes with β-NGF. |
