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384. MICMEN: Michaelis-Menten Enzyme Kinetics
by H. R. Pinnick, Jr., Department of Chemistry, Southeast Missouri State University, Cape Girardeau, Missouri 63701 The program provides for the treatment of enzyme systems which conform to the Michaelis-Menten kinetics theory.1,2 The program will handle kinetic data where there is no inhibitor as well as competitive inhibition, noncompetitive inhibition and uncompetitive inhibition. The data is linearized and the least-squares fit is performed on the three possible linear forms of the Michaelis-Menten equation. The three linear forms were chosen, since the advantages and limitations of each form are not the same. The decision of which linear form to use is left to the user. The three linear forms for the no inhibitor case are: (1) (2) (3) The equations for the three inhibition cases are described in the COMMENT cards of the program. _________ References: 1. R. Montgomery and C. S. Swenson, Quantitative Problems in the Biochemical Sciences, 2nd ed. (San Francisco: W. H. Freeman and Co., 1976), Chapter 11. 2. A. L. Lehninger, Biochemistry, 2nd ed. (New York: Worth Publishers, 1975), Chapter 8. _________ FORTRAN IV Lines of Code: 750 Recommended Citation: H. R. Pinnick, Jr., QCPE 13, 384 (1981). |