Abstract
Cell-free extracts of pig liver, yeast, and pea seeds catalyze a pyrophosphate-ATP exchange which is promoted to varying degrees by every amino acid and amide normally occurring in protein. Attainment of this exchange is markedly dependent upon the methods for preparation and assay of the enzymes. The preparations also catalyze the formation of amino acid hydroxamates and of apparent amino acid polynucleotide compounds. The amino acid-polynucleotide compounds are able to transfer their amino acid to the protein of isolated ribonucleoprotein particles in every case examined. The protein-bound amino acid can be removed by incubation with non-labeled amino acid-polynucleotide, but not with the free amino acid.
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