AMINO-ACID-SEQUENCE IN THE REACTIVE SITE REGION OF THE ACID-STABLE TRYPSIN, CHYMOTRYPSIN AND INTRACELLULAR PROTEINASES INHIBITOR FROM THE RABBIT SERUM

  • 1 January 1983
    • journal article
    • research article
    • Vol. 9  (2) , 193-199
Abstract
The thermo- and acid-stable trypsin, chymotrypsin and intracellular proteinase inhibitor (TAS-inhibitor) from rabbit serum was digested by trypsin, and the domain (MW 6200) with antitryptic activity was obtained in a homogeneous state. The N-terminal amino acid sequence of this domain was established by automatic Edman degradation. A high degree of homology for the primary structures from rabbit, human and bovine TAS-inhibitors was demonstrated.

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