Characterization of the cellular binding site for the urinary trypsin inhibitor.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference32 articles.
1. 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
2. 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
3. Elastase Inhibition by the Inter-α-Trypsin Inhibitor and Derived Inhibitors of Man and Cattle
4. Human Inter-α-Trypsin Inhibitor: Localization of the Kunitz-Type Domains in the N-terminal Part of the Molecule and their Release by a Trypsin-Like Proteinase
5. A Proteoglycan Related to the Urinary Trypsin Inhibitor (UTI) Links the two Heavy Chains of Inter-α-Trypsin Inhibitor
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