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Basic trypsin-subtilisin inhibitor from marine turtle egg white: hydrodynamic and inhibitory properties
P C Sil1, T K Chaudhuri, N K Sinha
1Department of Chemistry, Bose Institute, Calcutta, India.
Journal of Protein Chemistry
|February 1, 1993
Summary
A novel trypsin-subtilisin inhibitor was purified from marine turtle egg white. This inhibitor demonstrates potent, non-temporary inhibition of both trypsin and subtilisin via distinct binding sites.
Area of Science:
- Biochemistry
- Proteomics
- Marine Biology
Background:
- Protease inhibitors play crucial roles in regulating enzymatic activity.
- Marine organisms are a rich source of unique bioactive compounds.
Purpose of the Study:
- To isolate and characterize a novel protease inhibitor from marine turtle egg white.
- To elucidate the inhibitory mechanism and binding properties of the isolated inhibitor.
Main Methods:
- Purification using gel filtration and ion-exchange chromatography.
- Physicochemical characterization including molecular weight, isoelectric point, and hydrodynamic properties.
- Enzyme inhibition assays and chemical modification studies.
Main Results:
- Isolation of a homogeneous inhibitor with a single polypeptide chain (117 amino acids, 13,600 Da).
- The inhibitor lacks methionine and tryptophan, possesses an isoelectric point of pH 10.0, and exhibits specific hydrodynamic properties.
- Strong, non-temporary inhibition of trypsin and subtilisin through independent binding sites, with evidence of surface-exposed tyrosine residues.
Conclusions:
- The marine turtle egg white inhibitor is a potent and specific serine protease inhibitor.
- Its unique structural and binding characteristics offer insights into protease-inhibitor interactions.