The Measurement of Enzyme Kinetic Parameters of Poorly Soluble Substrates.
Technical rept. Nov 69-Oct 71,
EDGEWOOD ARSENAL MD
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A method is presented for determining enzyme kinetic constants using the full progress curve of conversion of substrate to products. Use is made of the integrated form of the Michaelis-Menten equation with correction for product inhibition. Satisfactory results were obtained with phenyl acetate using the enzyme acetylcholinesterase. Two computer programs are appended. One is for the calculation of enzyme kinetic constants using the integrated form of the rate equation. The second program is for calculation of the kinetic constants from initial rate data using the Wilkinson weighted regression method. A convenient procedure is suggested for the preparation of selected alcohols and thiols of limited stability, as, for example, phenol and thiocholine. Author