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- Title
- The specificity and catalytic properties of alu I methylase
- Author(s)
- Ho Sup Yoon; Hyang Suh; Ki Tae Kim; Moon Hi Han; Oook Joon Yoo
- Bibliographic Citation
- Korean Biochemical Journal, vol. 18, no. 1, pp. 88-93
- Publication 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.
- ISSN
- 0368-4881
- Publisher
- Korea Soc-Assoc-Inst
- Type
- Article
- Appears in Collections:
- 1. Journal Articles > Journal Articles
- Files in This Item:
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