1994Unpublished venueRequires access

Characterization of a Restriction Endonuclease, SdiI from Streptomyces diastatochromogenes

Moo Bae, Eunsook Song, Hye‐Yeon Hwang, Jeongbin Yim

Open publisher page 0 citations

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'

About this research paper

What this paper is about

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'

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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'

Key concepts: XhoI, Restriction enzyme, Isoschizomer, DNA, Restriction fragment, Streptomyces, Endonuclease, Enzyme

Related papers

Back to paper searchBrowse research topicsOriginal source
Characterization of a Restriction Endonuclease, SdiI from Streptomyces diastatochromogenes — Research Paper | ScholarLens