Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor.

Journal article

The interactions of three BPTI homologues with human leukocyte elastase and porcine pancreatic elastase have been investigated. The principal mutation in determining the specificity of inhibition was the Lys15-Val mutation at the P1 position. An additional mutation at P3, i.e., BPTI (Lys15-Val, Pro13-Ile), increased the inhibition of HLE to a Ki = 2.5 x 10(-10) M, but decreased the inhibition of PPE, showing this to be a useful site for improving selectivity. Kinetic evidence suggests that th...

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Authors: Kraunsoe, J; Claridge, T; Lowe, G

• Publication status: Published
• Journal: Biochemistry
• Volume: 35
• Issue: 28
• Pages: 9090-9096
• Publication date: 1996-07-01
• DOI: 10.1021/bi953013b
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Leukocyte Elastase; Recombinant Proteins; Animals; Swine; Magnetic Resonance Spectroscopy; Protein Binding; Aprotinin; Serine Proteinase Inhibitors; Amino Acid Sequence; Molecular Sequence Data; Pancreatic Elastase; Kinetics; Mutation; Cattle; Humans; Models, Chemical