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. Author manuscript; available in PMC: 2008 Aug 20.
Published in final edited form as: Biochemistry. 2007 Jan 23;46(3):883–889. doi: 10.1021/bi0616908

Figure 2.

Figure 2

A Kinetics of 5’-dA formation (approach to internal equilibrium) for holo-glutamate mutase reacting with d5-L-glutamate (10 mM). (•) Formation of [5’-H]-dA, as determined by 14C counts; (o) formation of [5’-3H]-dA, as determined by tritium counts. Each time point represents an average of three independent measurements. B Variation of the apparent α-secondary tritium kinetic isotope effect on 5’-dA formation as a function of time, showing the fit of the data to Equation 2..