Linked Life Data

799255

Source:http://linkedlifedata.com/resource/pubmed/id/799255

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1977-5-20
pubmed:abstractText
A method for the isolation of highly active Escherichia coli ribosomal subunits has been described and used to obtain 30S subunits, which are fully active in the cistron-specific binding of tRNA, and reassociated 70S ribosomes, which are at least 35% active in the synthesis of polypeptides. The dissociation constants (Kd) of the 30S-poly(U)-tRNAPhe complex, which proved to be practically identical for tRNAPhe in the deacylated and aminoacylated forms, as well as for the chemically synthesized peptidyl-tRNA, have been measured. Changes in the binding conditions (temperatures from 0 to 30 degrees, Mg2+ concentrations from 20 to 5 mM, and NH4+ concentrations from 200 to 50mM) have a significant effect on the value of Kd without altering the number of active 30S subunits. It has been shown that the codon-specific binding of tRNA to the 30S subunits is completely reversible. The 30S subunits are not only not inactivated after a single act of binding of a tRNA molecule, but are capable of undergoing this process repeatedly without any appreciable loss in activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
620-8
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:articleTitle
Isolation and study of some properties of the highly active 30S and 50S Escherichia coli ribosomal subunits.
pubmed:publicationType
Journal Article