Purification and Partial Properties of Trypsin Inhibitors in Garlic : A Review

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Two different trypsin inhibitors (inhibitors I and II) were isolated and purified from garlic (Allium scorodopum L.) by column chromatography on Sephadex G-50, Sephadex G-75, DEAE-cellulose and hydroxyl-apatite and by preparative disc electrophoresis. The purified inhibitors were found to be homogeneous by disc electrophoresis. The molecular weights of inhibitors I and II were calculated to be 3,000 and 3,100, respectively, by gel filtration on Sephadex G-50. It was clarified that inhibitors I and II contained 26 and 31 amino acid residues, respectively, and there was a major difference in half-cystine and glycine contents between the two inhibitors. Isoelectric points of inhibitors I and II were found to be pH 5.0 and pH 5.4, respectively, by isoelectric focusing. Inhibitor I was thermostable, while inhibotor II was thermolabile. Both inhibitors inhibited the enzymic activities of trypsin and plasmin competitively, but not of α-chymotrypsin, pepsin and kallikrein.
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