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- W2062610328 abstract "The functional properties of two forms of elongation factor 1 (EF-1) from the brine shrimp, Artemia salina, were compared. The heavy form of the factor (EF-1H) contains at least two different polypeptides and occurs in dried Artemia cysts. It showed little capacity to bind GTP to nitrocellulose filters (0.01 mol nucleotide/mol enzyme) and did not form a detectable complex with the nucleotide when subjected to gel filtration. No stable ternary complex between EF-1H GTP and aminoacyl-tRNA, was detected. EF-1L; which appears during the development of the shrimp embryo, consists of a single polypeptide chain of 53000 molecular weight. It bound GTP effectively to filters (0.15 mol nucleotide/mol enzyme) and the complex formed was stable to gel filtration. EF-1L formed a stable ternary complex with GTP and aminoacyl-tRNA. Despite these marked differences, both enzymes were comparable in the following assays: (a) polyphenylalanine synthesis; (b) catalytic activity in attaching aminoacyl-tRNA to ribosomes; (e) rate of attachment of aminoacyl-tRNA to ribosomes; (d) ribosome-dependent hydrolysis of [γ-32P]GTP Furthermore, preincubation of EF-1L with GTP and labelled aminoacyl-tRNA gave no competitive advantage in binding the aminoacyl-tRNA to ribosomes as compared to the same system without preincubation. These results suggested that ternary complex formation is not the ratelimiting step in the binding of aminoacyl-tRNA to ribosomes. The possible role of the additional polypeptide components of EF-1H in protein synthesis is discussed." @default.
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- W2062610328 date "1976-10-01" @default.
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- W2062610328 title "Characterization of Developmentally Regulated Forms of Elongation Factor 1 in Anemia salina. 2. Functional Properties of the Enzymes" @default.
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- W2062610328 doi "https://doi.org/10.1111/j.1432-1033.1976.tb10920.x" @default.
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