Studies on barley trypsin inhibitor. II. Structural changes induced by denaturants and their reversibility

No change in the activity of a trypsin inhibitor from barley was observed on treatment with heat and denaturants such as urea and guanidine hydrochloride. Thus, the conformational properties of the inhibitor were investigated. CD spectra of the native inhibitor were analysed on a curve-fitting technique using the data for poly-L-lysine...