Literature DB >> 8048957

Multiformity of elongation factor eEF-2 isolated from rat liver cells.

A Gajko1, W Gałasiński, A Gindzieński.   

Abstract

Two fractions of eEF-2 (M(r) approx. 100,000 and M(r) approx. 65,000) were isolated from post-ribosomal supernatant of the rat liver cells. Only eEF-2, with mol. weight of about 100,000 Da, can be phosphorylated, but only eEF-2, with mol. weight of about 65,000 Da, was isolated from the active polyribosomes. The existence of two eEF-2 forms with different properties in the rat liver cells is striking and uncovers new aspects for the cellular function of this protein.

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Year:  1994        PMID: 8048957     DOI: 10.1006/bbrc.1994.2007

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Elongation factor 2 as a target for selective inhibition of protein synthesis in vitro by the novel aromatic bisamidine.

Authors:  Anna Gajko-Galicka; Krzysztof Bielawski; Krystyna Sredzinska; Anna Bielawska; Andrzej Gindzienski
Journal:  Mol Cell Biochem       Date:  2002-04       Impact factor: 3.396

2.  Identification of elongation factor 2 as the essential protein targeted by sordarins in Candida albicans.

Authors:  J M Domínguez; J J Martín
Journal:  Antimicrob Agents Chemother       Date:  1998-09       Impact factor: 5.191

  2 in total

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