Independent heat stabilization of proteases associated with multiheaded inhibitors. Trypsins bound at nonequivalent sites on chicken ovoinhibitor.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. Determination of trypsin-inhibitor complex dissociation by use of the active site titrant, p-nitrophenyl p'-guanidinobenzoate
2. Evidence That the Two Binding Sites for Trypsin on Chicken Ovoinhibitor Are Not Equivalent
3. Preferred binding of bovine and porcine trypsins at two different sites on chicken ovoinhibitor. Reduced dissociation of mixed trypsin complexes.
4. Heat stabilization produced by protein-protein association. A differential scanning calorimetric study of the heat denaturation of the trypsin-soybean trypsin inhibitor and trypsin-ovomucoid complexes.
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1. Estimation of melting curves from enzymatic activity-temperature profiles;Biotechnology and Bioengineering;1993-11-20
2. Study of strong to ultratight protein interactions using differential scanning calorimetry;Biochemistry;1990-07-24
3. [6] Thermodynamic parameters for protein-protein and protein-ligand interaction by differential scanning microcalorimetry;Methods in Enzymology;1986
4. Interaction and thermal stability of fluorescent labeled derivatives of thrombin and antithrombin III;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1984-02
5. Stability of Enzyme Inhibitors and Lectins in Foods and the Influence of Specific Binding Interactions;Advances in Experimental Medicine and Biology;1984
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