Elongation Factor 1 from Artemia salina Properties and Disaggregation of the Enzyme

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Abstract
Elongation factor 1 has been purified from undeveloped embryos of Artemia salina. The purified enzyme appears to be an aggregate (molecular weight ∼ 200000) which on sodium dodecylsulfate gels shows the presence of two major protein bands whose estimated molecular weights are 52000 and 47000. Lipid material appears to be associated with the purified protein. In aminoacyl‐tRNA binding to ribosomes, there is only a limited turnover of the enzyme, but the protein acts catalytically in amino acid polymerization. The enzyme is disaggregated by a partially purified phospholipase C preparation, elastase and under certain conditions, by guanosine nucleotides. The significance of these results is discussed with respect to the overall role of elongation faction I in aminoacyl‐tRNA binding to ribosomes.