Characterization of sialytransferase in noncancerous and neoplastic human liver tissue.

When compared to uninvolved adjacent tissue, metastatic tumors in human liver appear to have significantly reduced sialytransferase activity. No significant kinetic differences (Michaelis constants, thermostability, and pH optima) between noncancerous and cancerous tissue sialytransferase were found. Mixing experiments between cancerous and noncancerous tissues indicated that inhibitors of sialytransferase activity were present in cancerous tissue. Subsequent experiments demonstrated increased levels of bound sialic acid in the tumor tissues. Inasmuch as futuin, a sialoglycoprotein, inhibits sialyltransferase activity, the increased levels of bound sialic acid in tumor tissue may be responsible for the reduced enzyme activity in these tissues.