Nerve growth factor biosynthesis: isolation and characterization of a guinea pig prostate kallikrein.
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.
D000595:Amino Acid Sequence; D000818:Animals; D006168:Guinea Pigs; D007610:Kallikreins / Q000302:isolation & purification* / Q000378:metabolism; D001121:Lysine Carboxypeptidase / Q000302:isolation & purification / Q000378:metabolism; D008297:Male; D008970:Molecular Weight; D009414:Nerve Growth Factors / Q000096:biosynthesis*; D011467:Prostate / Q000201:enzymology*
D009414:Nerve Growth Factors; D001121:Lysine Carboxypeptidase; D007610:Kallikreins