Kinetic and equilibrium characterization of the interaction between bovine trypsin and I-ovalbumin
Abstract
Serpins are a superfamily of structurally linked proteins with interesting functional properties. Most serpins act as proteinase suicide inhibitors and play a key role in a number of physiological processes. Structural flexibility properties make serpins extremely available to conformational transitions, often causing changes in protein function. Ovalbumin is a member of the serpin family that is not able to inhibit serine proteinases in its native form. In contrast, I-ovalbumin, the product of a heating transition, is a potent reversible serine proteinase inhibitor. In this paper, a detailed equilibrium and kinetic characterization of the interaction between the serpin ovalbumin and bovine trypsin, using a resonant mirror technique, is reported. This methodology revealed that the high affinity interaction between the two binding partners is characterized by high kinetic association constants and low kinetic dissociation constants. The modulation exerted by protons in solution, examined taking into account structural motifs characterizing the binding interface between the two macromolecules, suggests an interaction reminiscent of that observed for the binding of other serine proteases to their ligands.
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Erg11 catalyzes 14-methylation of lanosterol in C. albicans through three cycles, each requiring two electrons from NADPH-dependent Ncp1.
“Erg11, a cytochrome P450 enzyme, catalyzes the 14-methylation of lanosterol in C. albicans through three cycles13,14, each requiring two electrons from nicotinamide adenine dinucleotide phosphate (NADPH)-dependent Ncp1 reductase15,16.”
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“Erg11,acytochromeP450enzyme,catalyzesthe14-methylationof lanosterol in C. albicans through three cycles 13,14 , each requiring two electrons from nicotinamide adenine dinucleotide phosphate (NADPH)-dependent Ncp1 reductase 15,16 .”
- Authors
- Cuccioloni, M., Sparapani, L., Amici, M., Lupidi, G., Eleuteri, A. M., & Angeletti, M.
- Affiliations
- Università di Camerino (IT)
- Corresponding author
- Cuccioloni, Massimiliano
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 1702
- Issue
- 2
- Pages
- 199-207
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2035492984
- Cited by
- 8
- References
- 63
- Citations by year
- 2025: 1 · 2017: 2 · 2014: 1
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Unicam Scientific Publications (University of Camerino) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- bovine trypsin, serpins, serine protease inhibitors, protein-protein interaction kinetics, binding equilibrium, proton modulation, binding interface
- MeSH terms
- Animals, Cattle, Chickens, Hydrogen-Ion Concentration, Models, Theoretical, Ovalbumin, Protein Binding, Trypsin, Biosensing Techniques, Serine Proteinase Inhibitors, Surface Plasmon Resonance
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