Peking duck globin mRNA was purified from the total RNAs of reticulocytes by oligo (dT) -cellulose chromatography and sucrose gradient centrifugation. The purified 9S mRNA showed a single band on a polyacrylamide gel in 7mol/L urea. Their translation activities were measured in a wheat germ cell-free system. In comparison with the control, globin mRNA gave a 10-fold stimulation of 3H-leucine incorporation and the translated products were identified by sodium dodecyl sulfate gel electrophoresis as the authentic globin. Single and double stranded globin cDNA was synthesized from the purified 9S mRNA or reticulocyte poly(A) RNA with AMY reverse transcriptase and DNA polymerase I(Klenow fragment). The products were analyzed by polyacrylamide gel electrophoresis in 7mol/L urea. The lengths of the double stranded cDNA fragments were about 500 base pairs.