A modified cDNA of mature humam apolipoprotein A-II (apoA-II) was expressed by a sterol-uptake yeast strain (erg10) of Saccharomyces cerevisiae. ApoA-II cDNA was fused with a modified yeast alpha factor leader peptide coding sequence under phosphoglycerate kinase promoter control in a 2 micron-based plasmid construction. The use of cholesterol allowed apoA-II secretion in the culture medium. The mono and dimeric forms of apoA-II (approximately 3 micrograms per ml) were detected.