Protein isolates prepared from yeasts by isoelectric precipitation and ultrafiltration, respectively, show differences in their solubility and gelchromatographic behaviour. The ultrafiltrated preparation represents a less aggregated protein. The SDS-discelectrophoresis patterns are identical, which is a proof for an identical protein polypeptide distribution in the isoelectric precipitated and ultrafiltrated samples.Significant differences were found between ultrafiltrated proteins from Succhuromyces cerevisiae and Candidu guilliermondi yeasts using SDS-disc-electrophoresis, gel chromatography, as well as determination of solubility profiles, .amino acid composition, and thiol/disulphide content.All the main fractions of the isolated protein posses a molecular weight distribution mainly in the range of 50000-70000. The polypeptide patterns in the SDS-electrophoresis are characterized by a great number of zones in the molecular weight range of 10000-60000.