Injection of equivalent amounts of normal (PiMM) or abnormal (PiZZ) alpha 1-antitrypsin mRNA into Xenopus oocytes resulted in secretion of both the normal and abnormal alpha 1-antitrypsin. A much lower proportion of the abnormal protein was secreted, and the Z alpha 1-antitrypsin that was not secreted accumulated within the cell in a high-mannose form. The time taken for secretion of the normal and abnormal proteins was identical. Both the secreted and intracellular alpha 1-antitrypsin synthesized by oocytes were functionally active.