• Title/Summary/Keyword: Streptomyces diastatochromogenes

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Numerical Identification of a Streptomyces Strain Producing Restriction Endonuclease Sdi I (제한효소인 Sdi I을 생성하는 Streptomyces 분리 균주의 수리동정)

  • Bae, Moo;Suh, Won-Na;Song, Eun-Sook;Lee, Kye-Joon
    • Microbiology and Biotechnology Letters
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    • v.22 no.2
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    • pp.126-133
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    • 1994
  • Numerical identification was aplied for Streptomyces sp.264, an isolate producing a new restriction endonuclease Sdi I. The restriction enzyme would appear to be an isoschisomer of Xho I. Fifty taxonomic unit characters were tested and the data obtained were analyzed numerically by using the TAXON program. The isolate was identified to be the major cluster 19 of Streptomyces and best matched to S. diastatochromogenes. It was, therefore, concluded that the isolate was identified to be a member of Streptomyces diastatochromogenes.

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Purification of Festriction Endonuclease,SdiI, from Streptomyces diastatochromogenes (Streptomyces diastatochromogens로부터 제한효소 SdiI의 분리정제)

  • Bae, Mu;Song, Eun-Suk
    • Korean Journal of Microbiology
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    • v.32 no.4
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    • pp.297-300
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    • 1994
  • About thirty bacterial strains of actinomycete isolated from the soil were examined for the presence of restriction endonuclease activity. Streptomyces diastatochromogenes, which was identified previously, was found to contain restriction endonuclease activity. The purification of this enzyme, SdiI, was carried out via streptomycin sulfate precipitation and ammonium sulfate fractionation followed by hydroxylapatite column chromatography. Sephacryl S-200 HR column chromatography and second hydroxylapatite column chromatography. SDS-polyacrylamide gel electrophoresis of the active protein (purified from various column chromatography) resulted in 35,000 Da protein.

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Characterization of a Restriction Endonuclease, SdiI from Streptomyces diastatochromogenes (Streptomyces diastatochromogenes로부터 분리된 SdiI의 특성에 관한 연구)

  • Bae, Moo;Song, Eun-Sook;Hwang, Hye-Yeon;Yim, Jeong-Bin
    • Korean Journal of Microbiology
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    • v.32 no.4
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    • pp.301-305
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    • 1994
  • 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 $60^{\circ}C$ and 500 mM of NaCl concentration. It was stable between 20^{\circ}C$ and $60^{\circ}C$, and essentially requires $MgCl_2$ 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‘-C${\downarrow}$TCGA G-3' 3'-G AGCT${\uparrow}$C-5'

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