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.
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.
D000510:Alpha-Globulins / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002918:Chymotrypsin; D006801:Humans; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D014357:Trypsin / Q000378:metabolism; D014360:Trypsin Inhibitor, Kunitz Soybean; D014361:Trypsin Inhibitors
D000510:Alpha-Globulins; D010446:Peptide Fragments; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor; D014360:Trypsin Inhibitor, Kunitz Soybean; D002918:Chymotrypsin; D014357:Trypsin