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Steady-state kinetics of enzyme-catalyzed copolymerization on primers

✍ Scribed by V. Bloomfield

Publisher: Wiley (John Wiley & Sons)
Year: 1966
Tongue: English
Weight: 502 KB
Volume: 4
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.1966.360040608

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✦ Synopsis

The theory of the steady-state kinetics of irreversible enzyme-catalyzed homopolpmerization and copolymerization on primers has been developed. The rate law for homopolymerization is of the Michaelis-Menten form, but the kinetic parameters depend on primer concentration. Copolymerization has been treated for two monomers considering both terminal and penultimate effects and for four monomers considering terminal effects. The composition equations and conditional probabilities for monomer succession are identical for enzymatic and nonenzymatic processes, because the steadystate approximation is used in both cases. The reactivity ratios and steady-state velocities are different, however. Examination of published results for AU and UG copolymers synthesized by polynucleotide phosphorylase permits evaluation of reactivity ratios for the AU copolymer and indicates that penultimate effects may be operative in both cases.

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