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Sequence Studies on the α-, β-, and γ-Chains of Elongation Factor 1 from Artemia : Some Practical Notes

  • Chapter
Advanced Methods in Protein Microsequence Analysis

Abstract

In eukaryotic organisms, elongation factor 1 encloses three polypeptide chains, designated as EF-1α, EF-1ß and EF-1γ. EF-1α, a 51,000 MW protein, is the eukaryotic equivalent of the prokaryotic, aminoacyl tRNA-carrying enzyme EF-Tu. Both EF-1 α and EF-Tu can bind aminoacyl tRNA and GDP or GTP. EF-1 β, having a MW of 26,000, corresponds to prokaryotic EF-Ts, the enzyme that exchanges in the EF-Tu. GDP-complex, GDP for GTP. The function of EF-1γ, which has no prokaryotic counterpart, is still unknown. This protein, which has a MW of 46,000, is normally tightly associated with the ß-chain, forming the complex EF-1 βγ. In the brine shrimp Artemia, a high molecular weight complex between the three polypeptide chains can be isolated from dormant cysts; in the free-swimming nauplii, however, free EF-1α is found predominantly. The significance of the complexing of EF-1 α with the other two chains in dormant cysts is still unclear (for a recent review see [1]).

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Author information

Authors and Affiliations

  1. Sylvius Laboratories, Faculteit der Geneeskunde, Rijksuniversiteit Leiden, P.O. Box 9503, NL-2300, RA Leiden, The Netherlands

    R. Amons

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  1. R. Amons
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Editors and Affiliations

  1. Abteilung Wittmann, Max-Planck-Institut für Molekulare Biologie, Ihnestraße 63-73, D-1000, Berlin 33, Germany

    Brigitte Wittmann-Liebold

  2. Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Franklinstraße 29, D-1000, Berlin 10, Germany

    Johann Salnikow

  3. Institut für Biochemie, Freie Universität Berlin, Otto-Hahn-Bau, Thielallee 63, D-1000, Berlin 33, Germany

    Volker A. Erdmann

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© 1986 Springer-Verlag Berlin Heidelberg

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Amons, R. (1986). Sequence Studies on the α-, β-, and γ-Chains of Elongation Factor 1 from Artemia : Some Practical Notes. In: Wittmann-Liebold, B., Salnikow, J., Erdmann, V.A. (eds) Advanced Methods in Protein Microsequence Analysis. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71534-1_29

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  • DOI: https://doi.org/10.1007/978-3-642-71534-1_29

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-71536-5

  • Online ISBN: 978-3-642-71534-1

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