Abstract
Abstract When mouse reticulocyte 9 S RNA is incubated with either a heterologous mammalian (guinea pig) or an avian (duck) reticulocyte cell-free protein-synthesizing system, material is synthesized which co-chromatographs with authentic mouse α- and β-globin markers. Tryptic digests of these products, labeled with a mixture of 15 l-U-14C-amino acids, and authentic α- or β-globin were fingerprinted together. Comparison of authentic marker peptides, located by ninhydrin, and those directed by the mouse globin mRNA, located by autoradiography, demonstrates that most, if not all, of the tryptic peptides are synthesized, the NH2-terminal peptides lack methionine and the COOH-terminal peptides are terminated correctly. Thus, mouse reticulocyte 9 S RNA contains α- and β-globin mRNAs which are translated by both mammalian and avian cell lysates with a high degree of fidelity.
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