Thermodynamic measurements on the interaction of porcine trypsin with single- and two-chain trypsin inhibitors from corn seeds

Interactions Outside the Proteinase-binding Loop Contribute Significantly to the Inhibition of Activated Coagulation Factor XII by Its Canonical Inhibitor from Corn

“…Both the uncleaved one-chain and cleaved two-chain forms of CHFI are reported to inhibit trypsin (27, 28) and FXIIa (3, 4). However, the two-chain form exhibits only 20–25% of the activity of the one-chain form (3, 4).…”

Protease Inhibitors in Cereals

“…This procedure may modify the active site of the inhibitor by irreversible hydrolysis, when eluting from the chromatography column, giving a slower reacting or weaker inhibitor. Furthermore, the reported data indicate a partial destruction of the inhibitor during the elution process as both the native and modified inhibitor have been reported to be stoichiometric inhibitors (Burkhard et al, 1979). If the maize trypsin inhibitor had been purified by conventional methods the results might, therefore, have been different.…”