pubmed-article:1991042 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1991042 | lifeskim:mentions | umls-concept:C1262903 | lld:lifeskim |
pubmed-article:1991042 | lifeskim:mentions | umls-concept:C1621907 | lld:lifeskim |
pubmed-article:1991042 | pubmed:dateCreated | 1991-3-1 | lld:pubmed |
pubmed-article:1991042 | pubmed:abstractText | DNA methylase activity was detected in nuclei from pea shoots. The enzyme can only be extracted by low-salt treatment if the nuclei are pretreated with micrococcal nuclease. Only a single enzyme was detected, and it was purified to a specific activity of 1620 units/mg of protein. It has an Mr of 160,000 on gel filtration and SDS/PAGE. Pea DNA methylase methylates cytosine in all four dinucleotides, and this is interpreted to show that it acts on CNG trinucleotides. Although it shows a strong preference for hemi-methylated double-stranded DNA, it is also capable of methylation de novo. Homologous DNA is the best natural substrate. In vitro the enzyme interacts with DNA to form a salt-resistant complex with DNA that is stable for at least 4 h. | lld:pubmed |
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pubmed-article:1991042 | pubmed:language | eng | lld:pubmed |
pubmed-article:1991042 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1991042 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1991042 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1991042 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1991042 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:1991042 | pubmed:author | pubmed-author:RinaldiAA | lld:pubmed |
pubmed-article:1991042 | pubmed:author | pubmed-author:AdamsR LRL | lld:pubmed |
pubmed-article:1991042 | pubmed:author | pubmed-author:YesufuH MHM | lld:pubmed |
pubmed-article:1991042 | pubmed:author | pubmed-author:HanleyAA | lld:pubmed |
pubmed-article:1991042 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1991042 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1991042 | pubmed:volume | 273(Pt 2) | lld:pubmed |
pubmed-article:1991042 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1991042 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1991042 | pubmed:pagination | 469-75 | lld:pubmed |
pubmed-article:1991042 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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pubmed-article:1991042 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1991042 | pubmed:articleTitle | DNA methylase from Pisum sativum. | lld:pubmed |
pubmed-article:1991042 | pubmed:affiliation | Department of Biochemistry, University of Glasgow, U.K. | lld:pubmed |
pubmed-article:1991042 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1991042 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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