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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1978-12-27
|
| pubmed:abstractText |
Sphingomyelin, phosphatidylserine, bovine lecithin and phosphatidylethanolamine modify the thermal stabilization of H2B-DNA complexes, by inducing stabilization at 0.3 and 0.6 H2B : DNA weight ratios and destabilify the arrangement of nucleohistone is confirmed by ultrastructural analysis which indicates a competitive action of these molecules during the nucleoprotein assembly. A possible regulatory role of phospholipids on native chromatin is proposed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0300-8177
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
16
|
| pubmed:volume |
20
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
159-66
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:360047-Chromatin,
pubmed-meshheading:360047-DNA,
pubmed-meshheading:360047-Histones,
pubmed-meshheading:360047-Hot Temperature,
pubmed-meshheading:360047-Microscopy, Electron,
pubmed-meshheading:360047-Nucleic Acid Denaturation,
pubmed-meshheading:360047-Phospholipids,
pubmed-meshheading:360047-Protein Denaturation
|
| pubmed:year |
1978
|
| pubmed:articleTitle |
H2B nucleohistone-phospholipid interactions. Thermal denaturation and ultrastructural analysis.
|
| pubmed:publicationType |
Journal Article,
Review
|