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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.
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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.
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FORTRAN IV
Lines of Code: 750
Recommended Citation: H. R. Pinnick, Jr., QCPE 13, 384
(1981).
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