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YOLK PROTEINS OF THE SAND DOLLAR DENDRASTER EXCENTRICUS *

Yolk granules were isolated from eggs of the sand dollar Dendraster excentricus by density gradient centrifugation. Isolated granules were homogenous by the electron microscopic criterion. Proteins contained in the granules were analyzed by polyacrylamide gel electrophoresis under both denaturing and native conditions. SDS-polyacrylamide gel electrophoresis resolved the proteins into 3 size classes of polypeptides: molecular weights over 90,000, around 40,000, and around 30,000. PAS reagent stained only those polypeptides present in the size class with the highest molecular weights. A histochemical test for phosphoprotein was negative with any of the polypeptides. Triton X-100 gel electrophoresis revealed that proteins in the yolk granules fundamentally consisted one large molecular weight glycoprotein and a group of small proteins. Two-dimensional electrophoresis has shown that the glycoprotein is an oligomer consisting of glycoprotein subunits, and that all small proteins are monomers. The glycoprotein and small proteins may form lipoprotein complexes in the yolk granules.