Polypeptide composition of invertase-containing vesicles of Saccharomyces cerevisiae

Vesicles containing invertase activity were obtained from protoplast homogenates of Saccharomyces cerevisiae by differential centrifugation followed by gel chromatography. These vesicles were similar in size and shape to yeast coated vesicles, and appear to have a complex polypeptide composition. Most of these polypeptides were seemingly bound to the surface of the vesicular structures, being released by treatment with alkali. A protein with an electrophoretic mobility similar to that of yeast clathrin (molecular mass of 185 kDa) co-purified with vesicles containing invertase activity, and exhibited cross-reactivity with anti-mammalian (pig) clathrin antibodies.