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Kinetic analyses of divalent cation-dependent EcoRV digestions on a DNA-immobilized quartz crystal microbalance by Shuntaro Takahashi; Hisao Matsuno; Hiroyuki Furusawa; Yoshio Okahata is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Enzymatic digestion with a type IIP restriction endonuclease EcoRV was investigated on a DNA-immobilized 27-MHz quartz crystal microbalance (QCM). Real-time observations of both the enzyme binding process and the DNA cleavage process of EcoRV were followed by frequency (mass) changes on the QCM, which were dependent on divalent cations such as Ca 2+ or Mg 2+ . In the presence of Ca 2+ , the site-specific binding of EcoRV to DNA could be observed, without the catalytic process. On the other hand, in the presence of Mg 2+ , both the binding of the enzyme to the specific DNA (mass increase) and the site-specific cleavage reaction (mass decrease) could be observed continuously from QCM frequency changes. From time courses of frequency (mass) changes, each kinetic parameter, namely binding rate constants (k on ), dissociation rate constants (k off ), dissociation constants (K d ) of EcoRV to DNA, and catalytic rate constant (k cat ) of the cleavage reaction, could be determined. The binding kinetic parameters of EcoRV in the presence of Ca 2+ were consistent with those of the binding process followed by the cleavage process in the presence of Mg 2+ . The k cat value obtained by the QCM

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Author

Shuntaro Takahashi; Hisao Matsuno; Hiroyuki Furusawa; Yoshio Okahata

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)