Linked Life Data

6497388

Source:http://linkedlifedata.com/resource/pubmed/id/6497388

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-12-5
pubmed:abstractText
Previous studies have indicated that the high-molecular-weight form of elongation factor 1 (EF-1H) contained four subunits (alpha, beta, gamma, and delta). Using the conventional methods of gel-filtration and ion-exchange chromatography, various forms of elongation factor 1 (EF-1 alpha, EF-1 beta delta, EF-1 beta gamma delta) have been purified from rabbit reticulocyte lysate. The procedure described allows one to purify these factors from a single batch of lysate in sufficient amounts for physical and biochemical studies. EF-1 alpha is a single polypeptide of Mr 52,000, and has an isoelectric point of 9.1. EF-1 beta delta and EF-1 beta gamma delta are composed of two and three nonidentical polypeptides, respectively, as judged by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Both proteins can form stable aggregates in native conditions that can reach more than 2,000,000 Da. The isoelectric point for each polypeptide was determined; 5.8 for EF-1 beta, 5.5 for EF-1 gamma, and 4.8 for EF-1 delta. The activity of both proteins was compared on a molecular basis by their ability to stimulate EF-1 alpha in the poly(U)-directed synthesis of polyphenylalanine. On the basis of this assay EF-1 beta gamma delta is slightly more active than EF-1 beta delta. The similarity of the amino acid composition of EF-1 gamma and EF-1 delta and the molar ratio of alpha: beta: gamma: delta in EF-1H of approximately 1:1:0.5:0.5 have led to the conclusion that EF-1 delta is probably a breakdown product of EF-1 gamma, and that the native form of EF-1H probably contains only the alpha, beta, and gamma subunits.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
591-602
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Purification of various forms of elongation factor 1 from rabbit reticulocytes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't