“…The esters A-Ac-Gly-L-Lys-OMe, A-Ac-L-Lys-OMe, A-Ts-L-Arg-OMe, A'-Ac-Tyr-OEt, A-Z-Lys-ONp, and A-Z-L-Tyr-ONp and a tripeptide anilide Boc-Phe-Val-Arg-Na are hydrolyzed (Bing, 1969;Cooper & Ziccardi, 1976;Harpel, 1970; Nagaki & Stroud, 1969; Morgan & Nair, 1977). The turnover rate of these substrates by Cls is very slow compared with the activity of other enzymes such as trypsin, thrombin, and plasmin toward the same compounds (Cooper & Ziccardi, 1976;Morgan & Nair, 1977, Andrews et al, 1978. Like these enzymes, however, Cls is competitively inhibited by substituted benzamidines and phenylguanidine as well as a variety of N-a-blocked tyrosines (Bing, 1969;Andrews et al, 1978), further illustrating the hydrophobic and ionic nature of the implicating the importance of the Cls esteratic site (Stroud et al, 1965).…”