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Nerve growth factor biosynthesis: Isolation and characterization of a guinea pig prostate kallikrein

✍ Scribed by Joan C. Dunbar; Ralph A. Bradshaw

Publisher
John Wiley and Sons
Year
1985
Tongue
English
Weight
583 KB
Volume
29
Category
Article
ISSN
0730-2312

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✦ Synopsis

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 K,, for lysine and arginine synthetic substrates, although the V,,, for arginine is much greater than that for lysine. Amino-terminal sequence analysis has also revealed a marked degree of homology to mouse y-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to 7-NGF, however, the guinea pig enzyme does not appear to form stable complexes with 0-NGF.

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