[Immunoenzyme analysis of polyphosphatases from various compartments of yeast cells].

Antibodies against purified polyphosphatase from the Saccharomyces cerevisiae cell envelope inhibited the activity of this enzyme and the polyphosphatase activity of the cytosol, being without any effect on vacuolar and nuclear polyphosphatase activities from the same yeast species cells. Using immunoblotting, it has been shown that it is the 40 kDa polypeptide that binds to these antibodies in preparations of cell envelope and cytosolic polyphosphatase. The molecular mass of these polyphosphatases determined by other methods was almost indentical. The 72 and 40 kDa polypeptides bind to these antibodies in isolated vacuoles, while the 64 and 32 kDa polypeptides--in isolated nuclei.