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KMID : 0377619880530070433
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Korean Jungang Medical Journal
1988 Volume.53 No. 7 p.433 ~ p.439
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Purification and Characterization of Bal I Methylase From Brevibacterium albidum
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Abstract
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This study is attempt to purify and characterize Bal I methylase from Brevi-bacterium albidum.
Bal I methylase was purified by ammonium sulfate fractionation, phosphocellulose column chromatography, DEAE column chromatography and Sephadex G - 150 column chromatography. The specific activity of the enzyme was 1.43 x 105 units/mg of protein. Bal I methylase was maximally activated at pH 7.5. Mehtylation of pBR 322- DNA by Bal I methylase was maximal in the presence of 50 mM NaCl.
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