pubmed-article:954084 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:954084 | lifeskim:mentions | umls-concept:C1516511 | lld:lifeskim |
pubmed-article:954084 | lifeskim:mentions | umls-concept:C0175631 | lld:lifeskim |
pubmed-article:954084 | lifeskim:mentions | umls-concept:C2827662 | lld:lifeskim |
pubmed-article:954084 | lifeskim:mentions | umls-concept:C0079835 | lld:lifeskim |
pubmed-article:954084 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:954084 | pubmed:dateCreated | 1976-10-20 | lld:pubmed |
pubmed-article:954084 | pubmed:abstractText | Antibodies elicited in rabbits by chromatin and by purified histone H2B have been used to study the structure of chromatin by immunoelectron microscopy. Chromatin spread on grids reveals a structure of closely packed spherical particles with an average diameter of 104 A, arranged either in clusters or in linear arrays of beads, some of which have a supercoil-like arrangement. No DNA strings connecting the beads could be observed. Upon antibody binding, the diameter of the particles increases up to 300 A. This size is compatible with a model where one layer of gamma globulin molecules 110 A long encircles a sphere of chromatin 100 A in diameter. The presence of rabbit gamma globulins on the enlarged beads has been verified by the addition of ferritin-labeled goat anti-rabbit gamma globulins. Anti-chromatin sera which react with nonhistone proteins but not with free histones or DNA react with more than 95% of the beads; this suggests that most of the beads contain nonhistone proteins. Since the number of nonhistone proteins is large, it is improbable that each sphere contains a full complement of these proteins. We therefore suggest that the various chromatin spheres contain different types of nonhistone proteins. About 90% of the chromatin spheres reacted with antibodies to histone H2B, suggesting the most of the chromatin beads contain this type of histone. | lld:pubmed |
pubmed-article:954084 | pubmed:language | eng | lld:pubmed |
pubmed-article:954084 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:954084 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:954084 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:954084 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:954084 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:954084 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:954084 | pubmed:month | Feb | lld:pubmed |
pubmed-article:954084 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:954084 | pubmed:author | pubmed-author:SperlingRR | lld:pubmed |
pubmed-article:954084 | pubmed:author | pubmed-author:GoldblattDD | lld:pubmed |
pubmed-article:954084 | pubmed:author | pubmed-author:BustinMM | lld:pubmed |
pubmed-article:954084 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:954084 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:954084 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:954084 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:954084 | pubmed:pagination | 297-304 | lld:pubmed |
pubmed-article:954084 | pubmed:dateRevised | 2000-12-18 | lld:pubmed |
pubmed-article:954084 | pubmed:meshHeading | pubmed-meshheading:954084-M... | lld:pubmed |
pubmed-article:954084 | pubmed:meshHeading | pubmed-meshheading:954084-N... | lld:pubmed |
pubmed-article:954084 | pubmed:meshHeading | pubmed-meshheading:954084-H... | lld:pubmed |
pubmed-article:954084 | pubmed:meshHeading | pubmed-meshheading:954084-A... | lld:pubmed |
pubmed-article:954084 | pubmed:meshHeading | pubmed-meshheading:954084-C... | lld:pubmed |
pubmed-article:954084 | pubmed:meshHeading | pubmed-meshheading:954084-M... | lld:pubmed |
pubmed-article:954084 | pubmed:year | 1976 | lld:pubmed |
pubmed-article:954084 | pubmed:articleTitle | Chromatin structure visualization by immunoelectron microscopy. | lld:pubmed |
pubmed-article:954084 | pubmed:publicationType | Journal Article | lld:pubmed |
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