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Primary structure of elongation factor 1γ from Artemia
Author(s) -
Maessen G.D.F.,
Amons R.,
Zeelen J.P.,
Möller W.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80532-x
Subject(s) - elongation factor , protein primary structure , peptide sequence , amino acid , eukaryotic translation elongation factor 1 alpha 1 , complementary dna , ef tu , homology (biology) , methionine , elongation , antiserum , biology , microbiology and biotechnology , biochemistry , genetics , gene , antibody , transfer rna , ribosome , rna , materials science , ultimate tensile strength , metallurgy
Complementary DNA corresponding to elongation factor 1γ, which forms a complex with EF‐1β, has been cloned. A λgt11 cDNA library has been screened with an antiserum against EF‐1βγ. The derived amino acid sequence of EF‐1γ corresponds to 429 amino acids excluding the initiator methionine, which is absent in the mature protein. About half of the protein was sequenced by direct protein sequence analysis. No clear homology with any other protein was found.