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elongation factor

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e·lon·ga·tion fac·tor

proteins that catalyze the elongation of peptide chains during protein biosynthesis.
Synonym(s): transfer factor (3)
Farlex Partner Medical Dictionary © Farlex 2012

e·lon·ga·tion fac·tor

(ē-long-gā'shŭn fak'tŏr)
Proteins that catalyze the elongation of peptide chains during protein biosynthesis.
Synonym(s): transfer factor (3) .
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

elongation factor (EF)

one of a group of special proteins required for the elongation process in TRANSLATION.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
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References in periodicals archive
Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton.
ADP-ribosylation of elongation factor 2 by diphtheria toxin: NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.
Name of Corresponding Homologous gene after BLAST searching cDNA clone genomic clone (% nucleotide sequence identity) STUB1 9-1 Hordeum vulgare alpha-tubulin 3 (90%) accession number AJ132399 SPRP1 10-1,14-1 Zea mays proline-rich protein (84%) accession number Y17332 SAQ1 16-1 Zea mays plasma membrane MIP protein (pip2) (96%) accession number AF131201 SEF1[alpha] 19-1 Zea mays Elongation factor 1[alpha] (93%) accession number U76259 ACKNOWLEDGMENTS
An additional copy of the gene for elongation factor was inserted into the Drosophila genome; it was supposed to enhance protein synthesis at higher temperature.
Use of the human elongation factor 1 alpha promoter as a versatile and efficient expression system.
In a number of bacteria, these two genes are associated with a third gene that encodes the Bacterial Elongation Factor P, which is involved in protein production.
Our previous studies have shown that enolase, [alpha]- and [beta]-tubulin, and elongation factor 1[beta] are myosin-V binding partners by affinity isolation.
A relationship between the accumulation of elongation factor lA (eEF1A) and endosperm protein-bound lysine in cereals has been established (Habben et al., 1995; Sun et al., 1997).
Five enzymes/proteins were identified as being differentially expressed in the livers of ketotic cows: expression of 3-hydroxyacyl-CoA dehydrogenase type-2 (HCDH), acetylcoenzyme A acetyltransferase 2 (ACAT) and elongation factor Tu (EF-Tu) were down-regulated, whereas that of alpha-enolase and creatine kinase were up-regulated.
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