Purification and characterization of a heavy-metal-modulated nuclear protein from SV40-transformed cells

Sodium arsenite was found to stimulate an SV40-transformed BALB/c cell line (SVT2) to synthesize a 31-kDa protein within 2.5 h. This SVT2 protein was purified to homogeneity. It is a nuclear protein which appears to be associated with membranes because it is not extractable from nuclear membrane preparations by 2 M salt. It is highly hydrophobic, eluting from a reverse-phase HPLC column at a similar acetonitrile concentration as a previously described 31-kDa BALB/c-3T3 cell nuclear protein. However, digestion of highly purified BALB/c-3T3 and SVT2 cell proteins with V8 protease revealed nonidentical fragmentation patterns. Moreover, amino acid analysis of the two proteins was also dissimilar, indicating different primary structures