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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1989-10-26
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pubmed:abstractText |
Upon extensive digestion with DNAaseI of placenta chromatin matrix, previously "stripped" from its loosely-bound components by high-salt extraction, a fraction is obtained that contains almost no endogenous DNA methylase activity but whose DNA, if still included in this whole fraction--not if it has been purified to a protein-free condition--is a good substrate for externally added enzyme. This chromatin matrix can even cause a significant stimulation of methylation of single-stranded Micrococcus luteus DNA by placental methylase. In vivo, this phenomenon may have possible counterparts in the existence of highly-methylated regions of chromatin loops that appear to be protected by tightly-bound protein components from digestion of the "stripped loops" with DNAaseI.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5-Methylcytosine,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Cytosine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Modification Methylases
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pubmed:status |
MEDLINE
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pubmed:issn |
0163-4992
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
149-57
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2476222-5-Methylcytosine,
pubmed-meshheading:2476222-Chromatin,
pubmed-meshheading:2476222-Cytosine,
pubmed-meshheading:2476222-DNA,
pubmed-meshheading:2476222-DNA Modification Methylases,
pubmed-meshheading:2476222-Female,
pubmed-meshheading:2476222-Humans,
pubmed-meshheading:2476222-Kinetics,
pubmed-meshheading:2476222-Methylation,
pubmed-meshheading:2476222-Placenta,
pubmed-meshheading:2476222-Pregnancy,
pubmed-meshheading:2476222-Solubility
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pubmed:articleTitle |
A possible role of chromatin and tightly-bound chromatin proteins on enzyme-catalyzed methylation of DNA.
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pubmed:affiliation |
Dipartimento di Biopatologia Umana, Universitá di Roma, La Sapienza, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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