Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1981-9-15
pubmed:abstractText
The interaction of rat liver ribosomal proteins L6, L8, L19, S9, and S13 with 5.8 rRNA was characterized by nitrocellulose membrane filtration. Binding approached saturation with the five proteins; the apparent association constants (K'a), measured at 4 degrees C and 22 degrees C, ranged from 0.2 to 18 X 10(5) M-1. The molar ratio of ribosomal protein and rRNA in the complexes at saturation approximated 1, indicating there is one binding site for each of the five proteins on the nucleic acid. A number of ribosomal proteins, including some previously suspected from affinity chromatography of associating weakly, did not form a complex with 5.8 S rRNA.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7207-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Characterization of the binding of rat liver ribosomal proteins L6, L8, L19, S9, and S13 to 5.8 S ribosomal ribonucleic acid.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.