Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-8-28
pubmed:abstractText
The non-histone chromatin proteins (NHCp) from pig liver and kidney have been partially fractionated in non-denaturing conditions by the use of histone H3 immobilized on agarose and the fractions obtained have been analysed by SDS-polyacrylamide gel electrophoresis and amino acid analysis. At least six different fractions have been obtained by successive increases of the ionic strength of the medium. Few NHCp have been evidentiated with subunit molecular weights 55,000 and less than 30,000, which diaplay a remarkably high affinity for histone H3, and require 5 M urea to be displaced from the immobilized histone. The elution patterns of the NHCp from liver and kidney, although very similar, reveal some significant differences between the two tissues, which are undetectable by SDS-electrophoresis and which are most likely due to tissue specific proteins. This histone-affinity chromatography appears to be a promising approach for the analysis of specific histone-NHCp interactions, and as a first step for NHCp purification.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Fractionation of non-histone chromatin proteins from pig liver and kidney by means of immobilized histone H3.
pubmed:publicationType
Journal Article, Comparative Study