The extracellular proteinase (EPR) of Ctadidiz d b~~ was induced in a medium containing bovine serum albumin as sole nitrogen source. There were two intracellular forms in cells induced to produce EPR, a 43 kDa protein (EPR) and a 45kDa protein (cross-reacting material of EPR; CRM-EPR); these were detected by h d o t t h g Using anti-EPR antiserum. The 43 kDa protein (EPR) may be the same as the extracellular form judging by molecular mass, a d the 45 kDa protein (CRM-EPR) may be a precursor form of EPR. Many dense granules were observed by electron microscopy near the plasma membrane of the mother cells in EPR-producing cells. Both the 43 and 45 kDa proteins were recovered in a membrane fraction and were solubilized by Triton X-100. When the membrane fraction was further fractionated by sucrose d d t y gradient centrifugation, the 43 and 45 kDa proteins were differentially fractionated. This suggests that they were located in Merent membranebound structures and is consistent with an assumption that the 45 kDa protein is a preclvsor for EPR.