Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, V[1–4]. Attachments of Carbohydrates in the Human Urinary Trypsin Inhibitor Isolated by Affinity Chromatography
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm2.1981.362.2.1357/pdf
Reference9 articles.
1. 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
2. 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
3. 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
4. Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, IV. The Amino Acid Sequence of the Human Urinary Trypsin Inhibitor Isolated by Affinity Chromatography
5. Zur Charakterisierung der säurestabilen Proteaseninhibitoren aus Humanplasma
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