Substrate Hydrophobic Groups and the Maximal Rate of Enzyme Reactions

[1]  T. Kunitake,et al.  THE PRIMARY SPECIFICITY OF ALPHA-CHYMOTRYPSIN. ACYLATED AMINO ACID ESTERS WITH NORMAL ALKYL SIDE CHAINS. , 1965, Journal of the American Chemical Society.

[2]  B. Hofstee.  SOME ASPECTS OF THE SPECIFICITY OF FATTY ACID ESTERASES , 1964, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[3]  Miles Jl,et al.  THERMODYNAMICS OF THE SOLUTION PROCESS. SOME APPLICATIONS TO ENZYME CATALYSIS, AND INHIBITION OF ALPHA-CHYMOTRYPSIN BY AROMATIC HYDROCARBONS. , 1963 .

[4]  E. Boger,et al.  The relationship of enzyme inhibitory activity to the structure of n-alkylphosphonate and phenylalkyl-phosphonate esters. , 1963, Biochemistry.

[5]  W. J. Canady,et al.  Synthesis of some esters of hippuric acid, and their hydrolysis by α-chymotrypsin , 1962 .

[6]  G. Hein,et al.  An interpretation of the kinetic behavior of model substrates of alpha-chymotrypsin. , 1961, Proceedings of the National Academy of Sciences of the United States of America.

[7]  B. Hofstee.  Kinetics of chymotrypsin with a homologous series of n-fatty acid esters as substrates. , 1959, Biochimica et biophysica acta.

[8]  B. Hofstee.  Micelle formation in substrates of esterases. , 1958, Archives of biochemistry and biophysics.

[9]  B. Hofstee.  A homologous series of soluble n-fatty acid esters (C2-C10) as substrates for serum cholinesterase. , 1958, The Journal of pharmacology and experimental therapeutics.

[10]  H. Neurath,et al.  Acylation of the enzymatic site of delta-chymotrypsin by esters, acid anhydrides, and acid chlorides. , 1957, The Journal of biological chemistry.

[11]  B. Hofstee.  Fatty acid esters as substrates for trypsin and chymotrypsin. , 1957, Biochimica et biophysica acta.

[12]  B. Hofstee.  Specificity of esterases. IV. Behavior of horse liver esterase towards a homologous series of n-fatty acid esters. , 1954, The Journal of biological chemistry.

[13]  B. Hofstee.  Specificity of esterases. II. Behavior of pancreatic esterases I and II towards a homologous series of n-fatty acid esters. , 1952, The Journal of biological chemistry.