Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, II. Characterization of a Second Inhibitory Inactive Domain by Amino Acid Sequence Determination
- 1 January 1979
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 360 (2), 1297-1304
- https://doi.org/10.1515/bchm2.1979.360.2.1297
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.Keywords
This publication has 3 references indexed in Scilit:
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- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967
- The basic trypsin inhibitor of bovine pancreas. III. A progress report on the tryptic peptidesBiochemical and Biophysical Research Communications, 1964