Isolation and characterization of trypsin inhibitors from wheat germ.

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Abstract
Trypsin inhibitors were isolated from wheat germ and 2 major inhibitors (trypsin inhibitors I and II) were purified by various chromatographies including ion-exchange chromatographies on DEAE-Sephadex and CM[carboxymethyl]-Sephadex and gel filtration on Bio-gel and Sephadex. Both inhibitors were polypeptides composed solely of amino acids. In the presence of 1% SDS [sodium dodecyl sulfate], inhibitor I showed a single symmetrical sedimentation boundary of 1.6 S and a single band in SDS-gel electrophoresis, but in the absence of SDS, it tended to aggregate. Inhibitor II was homogeneous in gel electrophoresis and velocity sedimentation with or without SDS in the solutions. The MW of inhibitors I and II were approximately 16,000 and 10,000, respectively, by SDS-gel electrophoresis. Some other properties of the 2 inhibitors, including specific inhibitory activities, amino acid compositions and UV spectral properties are presented.

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