NERVE GROWTH-FACTOR BIOSYNTHESIS - ISOLATION AND CHARACTERIZATION OF A GUINEA-PIG PROSTATE KALLIKREIN

被引:14
作者
DUNBAR, JC
BRADSHAW, RA
机构
关键词
D O I
10.1002/jcb.240290405
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 argine 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 of mouse .gamma.-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to .gamma.-NGF, however, the guineapig enzyme does not appear to form stable complexes with .beta.-NGF.
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页码:309 / 319
页数:11
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