Purification and characterization of Alu I methylase

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Purification and characterization of Alu I methylase

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dc.contributor.author Yoon, Ho Sup
dc.contributor.author Suh, Hyang
dc.contributor.author Han, Moon H.
dc.contributor.author Yoo, Ook Joon
dc.date.accessioned 2012-10-08T01:02:18Z
dc.date.available 2012-10-08T01:02:18Z
dc.date.copyright 1985
dc.date.issued 2012-10-08
dc.identifier.citation Yoon, H. S., Suh, H., Han, M. H., & Yoo, O. J. (1985). Purification and characterization of Alu I methylase. Korean Biochemistry Journal., 18(1), 82-87.
dc.identifier.uri http://hdl.handle.net/10220/8716
dc.description.abstract Alu I methylase has been isolated from 300g (wet weight) cells of Arthrobacter luteus. After ammonium sulfate fractionation, the protein which has methylase activity was purified through phosphocellulose, DEAE-cellulose, Heparin agarose, and Hydroxylapatite column chromatography. The methylated DNA by the purified methylase was resistatnt against Alu I endonuclease. The purified Alu I methylase was essentially homogeneous as judged by 10% SDS-polyacrylamide gel electrophoresis, and the apparent subunit molecular weight was 56,000±1,000. The specific activity of the enzyme was 1.32 × 105 units per mg protein.
dc.language.iso en
dc.relation.ispartofseries Korean biochemistry journal
dc.rights © 1985 Springer Verlag. This is the author created version of a work that has been peer reviewed and accepted for publication by Korean Biochem. J., Springer Verlag. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://www.jbmb.or.kr/jbmbonline/18_1/list.html].
dc.subject DRNTU::Science::Biological sciences.
dc.title Purification and characterization of Alu I methylase
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.openurl http://www.jbmb.or.kr/jbmbonline/18_1/list.html
dc.description.version Accepted version

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