Isolation and characterization of the messenger RNAs for mouse embryonic globin chains.

Messenger RNAs for mouse embryonic globins were purified from yolk sac erythroid cells by oligodeoxythymidilate-cellulose chromatography and sucrose density centrifugation. Full-sized complementary DNA copies of embryonic globin mRNAs were synthesized. Acrylamide gel electrophoresis of these RNAs indicate an average molecular weight of 220 000, including a polyadenylated sequence of about 35 residues, as determined by hybridization to [3H]polyuridylate. The wheat-germ translation products of mRNAs have the size and the ionic characteristics of the four embryonic globin chains alpha, x, y and z. Hybridization kinetics in vast RNA excess were performed and compared to standard r0t curves of adult globin messengers, demonstrating a total base sequence complexity of about 880 000 daltons, that is four different RNA sequences of 220 000 molecular weight. The titration of embryonic globin cDNAs with increasing amounts of their complementary RNA templates indicates that the embryonic globin messengers were isolated at a high degree of purity.