Human Inter-α-Trypsin Inhibitor. Limited Proteolysis by Trypsin, Plasmin, Kallikrein and Granulocytic Elastase and Inhibitory Properties of the Cleavage Products
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm2.1979.360.2.1313/pdf
Reference13 articles.
1. The Inter-α-Trypsin Inhibitor as Precursor of the Acid-Stable Proteinase Inhibitors in Human Serum and Urine
2. Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, I. Determination of the Amino Acid Sequence of the Antitryptic Domain by Solid-Phase Edman Degradation
3. 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
4. Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, III. Sequence of the two Kunitz-Type Domains inside the Native Inter-α-Trypsin Inhibitor, Its Biological Aspects and also of Its Cleavage Products
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2. A Kunitz Type of Proteinase Inhibitor Isolated from Boar Seminal Vesicle Fluid;Andrologia;2009-04-24
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