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Kinetic and Thermodynamic Analysis of Leech-Derived Tryptase Inhibitor Interaction with Bovine Tryptase and Bovine Trypsin
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F. Erba
Published/Copyright:
July 5, 2005
Abstract
The interaction of leech-derived tryptase inhibitor (LDTI) with bovine liver capsule tryptase (BLCT) and bovine trypsin has been studied using both thermodynamic and kinetic approaches. Several differences were detected: (i) the equilibrium affinity of LDTI for BLCT (Ka = 8.9 × 105 M−1) is about 600-fold lower than that for bovine trypsin (Ka = 5.1 × 108 M−1); (ii) LDTI behaves as a purely non-competitive inhibitor of BLCT, while it is a purely competitive inhibitor of bovine trypsin. These functional data are compared with those previously reported for the LDTI binding to human tryptase, where tight inhibition occurs at two of the four active sites of the tetramer (Ka = 7.1 × 108 M−1). Amino acid sequence alignment of BLCT, human βIItryptase and bovine trypsin allows us to infer some possible structural basis for the observed functional differences.
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Published Online: 2005-07-05
Published in Print: 2000-11-15
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Purification and Cloning of Type A/B hnRNP Proteins Involved in Transcriptional Activation from the Rat spi 2 Gene GAGA Box
- Release of Ribosome-Bound 5S rRNA upon Cleavage of the Phosphodiester Bond between Nucleotides A54 and A55 in 5S rRNA
- Noncovalent Binding of Poly(ADP-Ribose) to Nuclear Matrix Proteins: Developmental Changes and Tissue Specificity
- Mutational Analysis of Two PWW Sequence Motifs in Human Aminoacylase 1
- Divergent Enzyme Kinetics and Structural Properties of the Two Human Mitochondrial Creatine Kinase Isoenzymes
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- Identification of the 50S Ribosomal Proteins from the Eubacterium Thermus thermophilus
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