Isolation of an acid protease from rabbit reticulocytes and evidence for its role in processing redox proteins during erythroid maturation

A protease which generates a soluble hemepeptide from bovine liver microsomal cytochrome $\text{b}{}_5$ has been isolated from the membrane fraction of rabbit reticulocytes. Inhibition by pepstatin and an acidic pH optimum indicate that the protease belongs to the acid protease class. Little cytochrome $\text{b}{}_5$-processing activity is observed in rabbit erythrocytes. We suggest that the protease may be involved in the processing which generates the proteins of the methemoglobin reduction system from their membrane-bound precursors during the maturation of the erythroid cell.