A peptide with a molecular weight of 8 kDa and an N-terminal sequence closely resembling that of ubiquitin was isolated from fruiting bodies of the mosaic puffball mushroom Calvatia caelata. The peptide was purified using a protocol that involved ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, and ion-exchange chromatography on Mono S. The peptide inhibited translation in the cell-free rabbit reticulocyte lysate system and exhibited N-glycosidase activity. It potently inhibited proliferation of spleen cells with an IC50 of about 100 nM as indicated by the suppression of [methyl-H-3]thymidine uptake. The viability of breast cancer cells was reduced to half at a ubiquitin concentration of about 100 nM.