Abstract
Heavy and light forms of elongation factor 1 (EF-1) from calf brain have been partially purified. The heterogeneous heavy species (EF-1H) with molecular weights of 2.5 × 105 to over 1 × 106 appears to be a complex or aggregate of the light form of the enzyme (EF-1L); the latter has a molecular weight of between 50,000 and 60,000. EF-1H but not EF-1L, contains significant amounts of free and esterified cholesterol. Although EF-1H and EF-1L are both active in aminoacyl-tRNA binding to ribosomes, EF-1L reacts with GTP and aminoacyl-tRNA more efficiently than EF-1H.
Keywords: cholesterol, protein synthesis
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