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J. Biol. Chem., Vol. 259, Issue 9, 5380-5383, May, 1984
PJ Isackson and RA Bradshaw
Tryptic and cyanogen bromide peptides accounting for approximately 85% of
the amino acid sequence of the alpha-subunit of mouse 7 S nerve growth
factor have been isolated and extensively sequenced. The partial structure
revealed a high degree of identity with the gamma-subunit (greater than
80%), which is an arginine esteropeptidase of the serine protease family.
However, the alpha-subunit does not cleave synthetic arginine ester or
peptide substrates nor is it labeled by diisopropylfluorophosphate. The
lack of catalytic activity may result from a Gly----His substitution near
the active site serine or from the blocked NH2 terminus.
The alpha-subunit of mouse 7 S nerve growth factor is an inactive serine protease
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