| First Author | Kristensen P | Year | 1998 |
| Journal | Biochem Biophys Res Commun | Volume | 245 |
| Issue | 3 | Pages | 810-4 |
| PubMed ID | 9588196 | Mgi Jnum | J:47340 |
| Mgi Id | MGI:1203323 | Doi | 10.1006/bbrc.1998.8510 |
| Citation | Kristensen P, et al. (1998) Purification and characterisation of a tissue specific elongation factor 1 alpha (EF-1 alpha 2) from rabbit muscle. Biochem Biophys Res Commun 245(3):810-4 |
| abstractText | 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. |
