this observation suggests that the electrostatic interactions existing between subunits i and iii are more rapidly weakened than those between subunits i and ii , probably because fewer lysyl residues are involved and/or there is greater accessibility to the chemical reagent . although completely inactive on the specific substrates of trypsin , chymotrypsin and elastase , subunit iii hydrolyzed p-nitrophenyl acetate at a rate similar to that of chymotrypsin but without any burst of p-nitrophenol , which indicates that the weakly functional active site of the subunit is not quite comparable to that of serine protease zymogens .
C0008742
chymotrypsin
C0036734
serine protease