Literature summary for 3.4.21.4 extracted from

Cuccioloni, M.; Sparapani, L.; Amici, M.; Lupidi, G.; Eleuteri, A.M.; Angeletti, M.
Kinetic and equilibrium characterization of the interaction between bovine trypsin and I-ovalbumin (2004), Biochim. Biophys. Acta, 1702, 199-207.

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Inhibitors

Inhibitors	Comment	Organism	Structure
I-ovalbumin	high affinity interaction of enzyme with I-ovalbumin, the product of a heating transition of ovalbumin which acts as a potent reversible serine proteinase inhibitor. Interaction is characterized by high kinetic association constants and low kinetic dissociation konstants	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Subunits

Subunits	Comment	Organism
More	high affinity interaction of enzyme with I-ovalbumin, the product of a heating transition of ovalbumin which acts as a potent reversible serine proteinase inhibitor. Interaction is characterized by high kinetic association constants and low kinetic dissociation konstants	Bos taurus

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Release 2023.1 (January 2023)