Optical biosensor study interaction between trypsin and trypsin inhibitor

   
Rachenkova N.I.1, Ivanov Yu.D.1 , Molnar A.A.1, Archakov  A.I.1

1. Institute of Biomedical Chemistry, Russian Academy of Medical Sciences
Section: Experimental/Clinical Study
PubMed Id: 16521823
Year: 2005  Volume: 51  Issue: 6  Pages: 617-625
The formation of complexes between trypsin (T) and soybean tripsin inhibitor (STI) was analyzed, using a two-channel IAsys* optical biosensor. The temperature dependence of complex formation (with its major parameters – the association rate constants (kon), the dissociation rate constants (koff) and the equilibrium constant (Kp)) was determined. The equilibrium constants obtained well correlate with those obtained by other methods. The association rate constant for the binding of T\STI complex increased with temperature, while the dissociation rate constant practically remained unchanged. The association and dissociation rate constant activation parameters were calculated from their concentration dependence. Based on the temperature dependence the activation energy, enthalpy and entropy of complex formation were calculated. It was shown that the entropy component plays a key role in T\STI interaction
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Keywords: optical biosensor, trypsin, soybean trypsin inhibitor, protein-protein interactions
Citation:

Rachenkova, N. I., Ivanov, Yu. D., Molnar, A. A., Archakov, , A. I. (2005). Optical biosensor study interaction between trypsin and trypsin inhibitor. Biomeditsinskaya khimiya, 51(6), 617-625.
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