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Trypsin inhibitors were isolated and partially purified from wheat grain, Beta variety. The procedure for determination of the inhibitory activity was simplified. This pertains shortening of the reaction time as well as quantitative decrease of components in the incubation mixture. The inhibitory fraction was salted out at 30-65% ammonium sulfate(More)
A homogenous trypsin inhibitor from wheat grain has been characterized. It is a protein of molecular weight 9105 Da and isoelectric point pI = 9.5. It belongs to arginine type inhibitors. The isolated inhibitor does neither inhibit native proteinases from wheat grain nor alpha-chymotrypsin, papein and pepsin. However, it inhibits some proteinases from(More)
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