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The specificity and catalytic properties of Alu I methylase.

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The specificity and catalytic properties of Alu I methylase.

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Title: The specificity and catalytic properties of Alu I methylase.
Author: Yoon, Ho Sup.; Suh, Hyang.; Kim, Kitae.; Han, Moon H.; Yoo, Ook Joon.
Copyright year: 1985
Abstract: The specific methylation site for Alu I methylase was the cytosine nucleotide in Alu I sequence. The position of the methylated cytosine nucleotide was determined by the chemical cleavage reactions of the Maxam-Gilbert DNA sequencing procedure. As expected, the methylated cytosine nucleotide bands were disappeared on C+ T and C lanes on 12% sequencing gels. Alu I methylase was maximally active at near pH 7.5 in the presence of 50 mM NaCl. The methylase did not require Mg++ for activity, and obeyed Michaelis-Menten Kinetics with respect to both AdoMet and DNA. At 37°C, the Km for AdoMet was 0.44 μM, that for the Alu I site of pBR 322 DNA was 4.03 nM, and the corresponding turnover numbers were 1.83 methyl transfer per minute per monomer and 1.61 transfers per minute per monomer, respectively.
Subject: DRNTU::Science::Biological sciences.
Type: Journal Article
Series/ Journal Title: Korean biochemistry journal
School: School of Biological Sciences
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].
Version: Accepted version

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