Cross-class inhibition of cysteine proteinases by serpins differs from serpin inhibition of serine proteinases primarily in that no stable serpin-cysteine proteinase complex can be demonstrated. This difference in reaction mechanism was elucidated by studies of the inactivation of the cysteine proteinases, papain and cathepsin L, by the serpin antithrombin. The two proteinases were inactivated ...

The transcriptome response of Tribolium castaneum larvae to dietary protease inhibitors was evaluated by whole-genome microarray analysis. RNA was isolated from guts of larvae fed control diet (no inhibitor), or diets containing 0.1% E-64 (cysteine protease inhibitor), 5.0% soybean trypsin inhibitor (STI, serine protease inhibitor), or a combination of 0.1% E-64 and 5.0% STI. Data were analyzed...

A novel inhibitor of cysteine proteinases has been isolated from fruit bodies of a mushroom Clitocybe nebularis. The inhibitor was purified to homogeneity by affinity chromatography and gel filtration, followed by reverse-phase high pressure liquid chromatography. The active inhibitor has an apparent molecular mass of about 34 kDa by gel filtration and by SDS-polyacrylamide gel electrophoresis ...