The human apoAI gene was expressed in E. coli by in-frame fusion to a modified beta-galactosidase gene present in plasmid pUR291. The fused beta-galactosidase-apoAI gene product was expressed at a high level and was recognized by an anti-human apoAI antiserum. Besides the fused protein, at least one degradation product having an Mr similar to that of beta-galactosidase was present in high amounts in bacterial extracts. These results and those of a pulse-chase experiment indicate that degradation took place only in the apoAI moiety of the chimeric protein.