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- W2092248850 abstract "The binding of the MboII restriction endonuclease (R·MboII; ENase) to DNA containing its recognition site was investigated using a mobility shift assay. R·MboII forms specific, stable and immunodetectable complexes with its canonical target sequence. The association constant (Ka) of R·MboII was calculated to be 2.8 × 109/M, and is about 104-fold higher than the Ka value for non-specific binding. Based on results obtained after sedimentation of the R·MboII-DNA complex in a glycerol gradient and measurement of the retardation of the complexes in polyacrylamide gels, we conclude that specific binding to the canonical sequence involves a monomer of R·MboII. DNase I footprinting has shown that the enzyme covers 16 nucleotides of DNA on the 5′-GAAGA-3′ strand." @default.
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- W2092248850 date "1988-12-01" @default.
- W2092248850 modified "2023-10-16" @default.
- W2092248850 title "Properties and subunit structure of EcoRV methyltransferase" @default.
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- W2092248850 doi "https://doi.org/10.1016/0378-1119(88)90255-7" @default.
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