Thermodynamics of alpha-chymotrypsin-substrate and inhibitor complex formation as a function of pH. Hydrophobic binding by the low and high pH forms of the enzyme.
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Binding Sites↗
Biomedical subjects
W J Canady
Publications and source records attributed to W J Canady.
Thermodynamics of alpha-chymotrypsin-inhibitor complex formation. Effects of structural modification of the inhibitor.
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Alcohols↗
Spectrophotometric and kinetic evidence for the existence of at least two salt-dependent conformations of alpha-chymotrypsin at pH values near neutrality.
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Chymotrypsin↗
Solvent effects on human C'1-esterase.
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1-Propanol↗
A common size parameter for hydrophobic binding of inhibitors by alpha-chymotrypsin, alkylated alpha-chymotrypsin, and yeast alcohol dehydrogenase.
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Alcohol Oxidoreductases↗
A hydrocarbon-water model for the formation of the enzyme-inhibitor complex in the case of alpha-chymotrypsin.
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Acetophenones↗