Redpath, N.T. and Price, N.T. and Proud, C.G. (1996) Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase. Journal of Biological Chemistry, 271 (29). pp. 17547-17554. ISSN 0021-9258.
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A cDNA from rat skeletal muscle encoding calcium/calmodulin-dependent eukaryotic elongation factor-2 kinase (eEF-2K) has been cloned and sequenced, and the amino acid sequence of the protein has been deduced. The kinase is composed of 724 amino acids and has a predicted molecular mass of 81,499 Da. The cDNA was judged to be full-length, as the protein, expressed in rabbit reticulocyte lysate or wheat germ extract, migrated upon SDS-PAGE with the same apparent molecular weight as the purified kinase and possessed eEF-2K activity, eEF-2K contains all of the 12 catalytic subdomains present in the majority of protein kinases, but they are atypical and display only limited homology with other kinases. A putative calmodulin-binding domain is present C-terminal to the catalytic domain as is a putative pseudosubstrate sequence. Two antipeptide antibodies raised against sequences derived from a partial rabbit cDNA clone, cross-reacted with purified eEF-2K, and one also immunoprecipitated eEF-2K activity from cell extracts. Northern blot analysis demonstrated that eEF-2K mRNA is expressed in a number of different tissues and that it may exist in multiple forms.
|Subjects:||Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||F.D. Zabet|
|Date Deposited:||08 May 2009 15:22|
|Last Modified:||08 May 2009 15:22|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/18753 (The current URI for this page, for reference purposes)|
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