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  • Title: Purification and some properties of a proteinase inhibitor (DE-1) from Peltophorum africanum (weeping wattle) seed.
    Author: Joubert FJ.
    Journal: Hoppe Seylers Z Physiol Chem; 1981 Nov; 362(11):1515-21. PubMed ID: 7309008.
    Abstract:
    A proteinase inhibitor (DE-1) from the seed of Peltophorum africanum (Weeping wattle) was purified by chromatographic procedures involving Sephadex G-50, DEAE-cellulose and DEAE-Sepharose. It comprises 162 amino acid residues (molecular mass 18 000 Da) including 4 half-cystine residues and resembles the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-1 showed homology with Kunitz soybean trypsin inhibitor and also with the proteinase inhibitors from Albizzia julibrissin and Erythrina latissima seeds. The inhibitor stoichiometrically inhibited trypsin and also alpha-chymotrypsin in the molar ratio of 1:1 and represents, therefore, a Kunitz-type double-headed proteinase inhibitor.
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