Inhibition mechanism of a peanut trypsin-chymotrypsin inhibitor, B-III: Determination of the reactive sites for trypsin and chymotrypsin.

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Peanut inhibitor B-III was found to form two types of complexes with trypsin, T2I and TI, by gel filtration HPLC. Two cleaved peptide bonds, Arg (10)-Arg (11) and Arg (38)-Ser (39), in the trypsin modified inhibitor (TM-B-III_??__??_) (J. Biochem. 93, 479-485 (1983)) were resynthesized by the complex formation with 2 mol of trypsin. These results suggest that the two peptide bonds may be the reactive sites for trypsin. TM-B-III_??__??_ inhibited bovine trypsin as well as native B-III but had little chymotrypsin inhibitory activity.<br> The two peptide bonds, Arg (10)-Arg (11) and Arg (38)-Ser (39), in B-III were cleaved partly by prolonged incubation with a catalytic amount of chymotrypsin. But gel filtration HPLC of the chymotrypsin-inhibitor complex showed the formation of only CI complex. Incubation of TM-B-III_??__??_ with an equimolar amount of chymotrypsin resulted in the resynthesis of only the Arg (10)-Arg (11) bond. These findings suggest that Arg (10)-Arg (11) may be a true reactive site for chymotrypsin. An inhibition mechanism of B-III against trypsin and chymotrypsin was proposed from the results obtained by the present studies.

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