Abstract
Five variants of BTI-CMe1, the major trypsin inhibitor from Bomi barley endosperm, have been isolated and characterized. Three isoforms (designated BTI-CMe2.1, -CMe2.2 and -CMe2.3) were purified from Hordeum vulgare cv. Hatif de Grignon and two (named BTI-CMe3.1 and -CMe3.2) from cv. Valticky. Amino acid substitutions in their N-terminal sequences with respect to that of BTI-CMe1 were found in four of the variants. When the isolated proteins were tested against bovine trypsin, all were inhibitory, but they could be grouped in three classes (BTI-CMe3.1/-CMe3.2, BTI-CMe1/-CMe2.1 and BTI-CMe2.2/-CMe2.3) according to their levels of anti-tryptic activity. The barley trypsin inhibitor variants were not effective towards α-amylases from storage cereal pests ( Tenebrio molitor, Tribolium castaneum and Sitophilus oryzae), except for the case of BTI-CMe2.1, which showed a weak activity against the T. molitor enzyme.
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