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Evidence for multiple interacting binding sites in bovine tryptase

L Fiorucci¹, F Erba, M Coletta

¹Department of Experimental Medicine and Biochemical Sciences, University Tor Vergata, Rome, Italy.

|April 17, 1995

Summary

Bovine pancreatic trypsin inhibitor (BPTI) interacts with bovine tryptase, revealing a functional unit with at least four binding sites. These sites show complex interplay, influencing inhibitor and substrate binding, particularly with BPTI.

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Area of Science:

Biochemistry
Enzymology
Molecular Biology

Background:

Bovine pancreatic trypsin inhibitor (BPTI) and bovine tryptase are co-localized in bovine mast cell granules.
Understanding their interaction is crucial for mast cell function and protease regulation.

Purpose of the Study:

To analyze the interaction between BPTI and bovine tryptase.
To elucidate the binding characteristics and functional interplay of bovine tryptase's binding sites.

Main Methods:

Enzyme kinetics and inhibitor binding assays were performed.
Experiments were conducted at 30°C in 0.1 M Tris-HCl buffer at pH 8.0.

Main Results:

The functional unit of bovine tryptase possesses at least four binding sites for BPTI.

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Small inhibitors and substrates exhibit simple binding, while BPTI binding is heterogeneous.

BPTI presence induces positive functional interaction among binding sites for small inhibitors like benzamidine.

Conclusions:

Bovine tryptase's functional unit exhibits complex interplay among its binding sites.
This interplay is transmitted through secondary specificity sites, affecting inhibitor and substrate binding.
The findings provide insights into protease-inhibitor dynamics in mast cells.