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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
1981-1-26
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pubmed:abstractText |
The binding curves of histones H1 and H5 to chromatin in nuclei have been determined by a novel method which utilises the differential properties of free and bound histones on cross-linking with formaldehyde. The dissociation is thermodynamically reversible as a function of [NaCl]. The binding curves are independent of temperature over the range 4 degrees - 37 degrees C and independent of pH over the range 5.0 to 9.0. The curves are sigmoid, indicating co-operative dissociation with NaCl. The standard free energy of dissociation in 1 M NaCl for H1 is 0.5 Kcals/mole and for H5 is 3.5 Kcals/mole.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-1061151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-1064861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-1112409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-1175645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-1175657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-1236150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-13929115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-26067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-300680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-350271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-353875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-353876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-4291873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-4530301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-4554987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-465459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-4736702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-4861938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-5345975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-5459534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-5528231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-565920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-724497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-836274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-928061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7433099-986949
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3535-51
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1980
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pubmed:articleTitle |
The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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