Purification and characterisation of a tissue specific elongation factor 1 alpha (EF-1α2) from rabbit muscle

被引:12
作者
Kristensen, P
Lund, A
Clark, BFC
Cavallius, J
Merrick, WC
机构
[1] Univ Aarhus, Dept Chem, Div Biostruct Chem, Aarhus, Denmark
[2] Case Western Reserve Univ, Sch Med, Dept Biochem, Cleveland, OH 44106 USA
关键词
D O I
10.1006/bbrc.1998.8510
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The peptide elongation factor 1 alpha (EF-1 alpha) has been isolated and characterised from a number of species. Recently we and others have reported the existence of an isoform of the ubiquitously expressed EF-1 alpha mRNA in higher eukaryotes, including human cells. This isoform has a tissue specific expression pattern, confining it primarily to muscle, heart, and brain. In the present study we have purified the isoform of EF-1 alpha from rabbit muscle. Using partial amino acid analysis, we can conclude that in rabbit muscle essentially only the isoform of elongation factor 1 alpha, designated EF-1 alpha 2, is translated. Preliminary activity assays show that the isoform has the same functional activities as the normal EF-1 alpha, designated EF-1 alpha 1, in relation to protein synthesis, but may behave differently in the ability to bind nucleotides. Based on the availability of the isoforms of EF-1 alpha purified from a mammalian species, it will be possible to conduct further comparative studies in order to elucidate the different functions of EF-1 alpha 1 and EF-1 alpha 2 proteins. (C) 1998 Academic Press.
引用
收藏
页码:810 / 814
页数:5
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