Calorimetric Investigation of Chymotrypsin Ionization Reactions

  • Charles J. Martin
  • Bangalore R. Sreenathan
  • Mario A. Marini


On the basis of a series of investigations concerned with the effect of formaldehyde on chymotrypsin-catalyzed reactions, the cumulative evidence has led to the interpretation that formaldehyde is an active site label and forms an N-hydroxymethyl derivative with the imidazole moiety of the histidine residue, presumably His-57, involved in the rate-determining step for the catalysis of acylated aromatic amino acid esters. The consequence of this is that chymotrypsin becomes a less efficient catalyst (about 8-fold) although all active sites remain functional. The evidence leading to this conclusion has been presented in several publications (1–7), and encompasses experimental approaches involving Potentiometrie titration, kinetic, and spectroscopic studies.


Ionizable Group Titratable Group Imidazole Moiety Dissociable Group Base Uptake 
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Copyright information

© Springer Science+Business Media New York 1974

Authors and Affiliations

  • Charles J. Martin
    • 1
  • Bangalore R. Sreenathan
    • 1
  • Mario A. Marini
    • 2
  1. 1.Department of Biochemistry, The Chicago Medical SchoolUniversity of Health SciencesChicagoUSA
  2. 2.Department of BiochemistryNorthwestern University Medical and Dental SchoolsChicagoUSA

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