Elastase Inhibition by the Inter-α-Trypsin Inhibitor and Derived Inhibitors of Man and Cattle
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm2.1983.364.2.1703/pdf
Reference19 articles.
1. 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
2. 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
3. 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
4. The Amino Acid Sequence of the Double-Headed Proteinase Inhibitor from Canine Submandibular Glands, III. Sequencing studies
5. Synthesis and Analytical Use of 3-Carboxypropionyl-alanyl-alanyl-valine-4-nitroanilide: A Specific Substrate for Human Leukocyte Elastase
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