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  • Title: Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, II. Characterization of a second inhibitory inactive domain by amino acid sequence determination.
    Author: Wachter E, Hochstrasser K, Bretzel G, Heindl S.
    Journal: Hoppe Seylers Z Physiol Chem; 1979 Sep; 360(9):1297-303. PubMed ID: 92448.
    Abstract:
    A short digestion with excess of trypsin releases an inhibitor with an apparent molecular weight of 14,000 from both the inter-alpha-trypsin inhibitor and the ITI-related acid-stable inhibitor. The amino acid sequence of this inhibitor was determined. The inhibitor is composed of two covalently linked homologous Kunitz-type domains. One domain has antitryptic activity, as reported. This paper characterizes the second, inactive domain as also of the Kunitz type.
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