Characterization of a Restriction Endonuclease, SdiI from Streptomyces diastatochromogenes
Moo Bae, Eunsook Song, Hye‐Yeon Hwang, Jeongbin Yim
Abstract
Moo Bae, Eunsook Song, Hye‐Yeon Hwang, Jeongbin Yim
Abstract
In catalytic properties of the restriction enonuclease, SdiI, which was purified from Streptomyces diastatochromogenes, this enzyme was active at wide range between pH 7.0 and 12.5, and up to and 500 mM of NaCl concentration. It was stable between and , and essentially requires for endonuclease activity. The restriction map of lambda DNA which was obtained by double digestion with various enzymes suggested SdiI to be an isoschizomer of XhoI. From the determination of restriction site based on DNA sequencing method, recognition and cleavage specificity of SdiI was concluded as: 5‘-CTCGA G-3' 3'-G AGCTC-5'
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In catalytic properties of the restriction enonuclease, SdiI, which was purified from Streptomyces diastatochromogenes, this enzyme was active at wide range between pH 7.0 and 12.5, and up to and 500 mM of NaCl concentration. It was stable between and , and essentially requires for endonuclease activity. The restriction map of lambda DNA which was obtained by double digestion with various enzymes suggested SdiI to be an isoschizomer of XhoI. From the determination of restriction site based on DNA sequencing method, recognition and cleavage specificity of SdiI was concluded as: 5‘-CTCGA G-3' 3'-G AGCTC-5'
Key concepts: XhoI, Restriction enzyme, Isoschizomer, DNA, Restriction fragment, Streptomyces, Endonuclease, Enzyme