Comparison of Protein Sulfation in Control and Virus-Transformed Baby Hamster Kidney Cells

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Protein sulfation in baby hamster kidney cells (BHK) and their polyoma virus transformants (PY-BHK) was studied comparatively. On in vivo labeling, [³⁵S] -sulfate was incorporated into the 50K protein and proteins in the 100-180K range, represented by the 155K protein. The incorporation into both the 50K and 155K protein was elevated 2-3 fold in PY-BHK cells compared to in BHK cells. Tyrosine-O-sulfate was the only identifiable sulfated amino acid in both proteins. On in vitro labeling with [³⁵S] 3'-phosphoadenosine 5'-phosphosulfate (PAPS), at least 6 radioactive protein bands were discernible on gel electrophoresis. Of these, sulfation of the 57K and 60K proteins was elevated in PY-BHK cells compared to in BHK cells, whereas sulfation of the 39K protein was depressed in PY-BHK cells. Tyrosine-O-sulfate was the only identifiable sulfated amino acid in these proteins.