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  • Title: Isolation and characterization of a proteinase inhibitor from marama beans.
    Author: Elfant M, Bryant L, Starcher B.
    Journal: Proc Soc Exp Biol Med; 1985 Nov; 180(2):329-33. PubMed ID: 3850610.
    Abstract:
    A protease inhibitor was purified from the African marama bean (Tylosema esculenturm). The inhibitor is present in large amounts, representing about 10.5% of the total protein. The molecular weight is slightly larger than soybean trypsin inhibitor and was estimated at 23,000 by SDS-gel electrophoresis or 24,500 by amino acid analysis. The amino acid composition was atypical of most other plant inhibitors with a cysteine content of only one or possibly two residues/mole and a blocked amino terminus. Inhibition studies indicated virtually no inhibition of chymotrypsin activity. Elastase, however, was inhibited to the same extent as trypsin, requiring about 2 moles of inhibitor for complete inhibition of the enzyme.
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