Abstract
The major spore coat proteins (SP60, SP70, and SP96) of Dictyostelium discoideum have been analyzed by using two-dimensional nonequilibrium pH gradient electrophoresis. These proteins have been characterized with respect to electrophoretic behavior, metachromatic staining with silver, and posttranslational modifications; these techniques allow unambiguous identification of these proteins in silver-stained gels and autofluorograms of total cell extracts. They are synthesized by cells in the prespore region of migrating slugs, ultimately becoming major components of mature spores, but are not detectable either in cells in the prestalk region of slugs or in mature stalk cells. The ease with which these relatively abundant proteins can be recognized on two-dimensional gels makes them very useful markers for spatial and temporal differentiation in this organism.