Abstract
A major trypsin inhibitor (BTI-I) was purified from broccoli, Brassica oleracea, by conventional methods. BTI-I had a molecular weight of 8000 and an isoelectric point of 5.2. BTI-I inhibited bovine and porcine trypsins in an 1:1 (M/M) stoichiometry: the approximate Ki’s were 6 x 10 -11 M in both cases. The chemical modification suggested that BTI-I had an Arg-X bond as a trypsin reactive-site.
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