Purification and characterization of Alu I methylase
Yoon, Ho Sup
Han, Moon H.
Yoo, Ook Joon
Date of Issue1985
School of Biological Sciences
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.
Korean biochemistry journal
© 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].