Isothermal titration calorimetry determination of individual rate constants of trypsin catalytic activity

Author:

Aguirre César,Condado-Morales Itzel,Olguin Luis F.,Costas Miguel

Funder

CONACYT

DGAPA–UNAM

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference57 articles.

1. MEROPS: the database of proteolytic enzymes, their substrates, and inhibitors;Rawlings;Nucleic Acids Res.,2012

2. Electrostatic complementarity within the substrate-binding pocket of trypsin;Graf;Proc. Natl. Acad. Sci. U.S.A.,1988

3. The kinetics of the amidase and esterase activities of trypsin;Schwert;J. Biol. Chem.,1949

4. Differential specificities of thrombin, plasmin, and trypsin with regard to synthetic and natural substrates and inhibitors;Weinstein;Biochim. Biophys. Acta,1972

5. The preparation and properties of two new chromogenic substrates of trypsin;Erlanger;Arch. Biochem. Biophys.,1961

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