Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1982-10-29
pubmed:abstractText
Antibodies to the folding domain (residues 22-100) of histone H5 were elicited in rabbits. Analysis of the specificity of these antibodies by enzyme-linked immunoassay and by diazobenzyloxymethyl cellulose transfer techniques revealed that the antibody cross-reacts strongly with intact H5 and histones H1(0)a and H1(0)b purified from ox liver but not with the four core calf thymus, or with high mobility group proteins. We conclude that the globular region of H5 is serologically homologous to that of H1 degrees and suggest that possible functional similarities between the two proteins reside in this region.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10533-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Antibodies against the folding domain of histone H5 cross-react with H1(0) but not with H1.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't