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Nerve growth factor biosynthesis: Isolation and characterization of a guinea pig prostate kallikrein
Author(s) -
Dunbar Joan C.,
Bradshaw Ralph A.
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240290405
Subject(s) - guinea pig , kallikrein , isolation (microbiology) , biosynthesis , prostate , nerve growth factor , biology , chemistry , microbiology and biotechnology , endocrinology , biochemistry , medicine , enzyme , receptor , cancer
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 m for lysine and arginine synthetic substrates, although the V max 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.