Some properties of sialyltransferase in plasma and lymphocytes of patients with chronic lymphocytic leukemia.
Some properties of sialyltransferase activity in plasma and lymphocytes from patients with chronic lymphocytic leukemia were compared. Three distinct enzyme fractions were identified in plasma: (1) cation independent, irreversibly bound to agarose; (2) cation dependent, weakly bound to agarose; (3) strongly bound to agarose, lost upon dialysis. Lowering of the peripheral lymphocyte count by leukapheresis markedly decreased the level of serum sialyltransferase, suggesting the circulating lymphocyte is a source of the serum enzyme. The enzyme solubilized by detergent from lymphocytes showed a substantially lower Km for CMP-sialic acid than did the serum enzyme, was less sensitive to several inhibitors, was not irreversible bound to Agarose, and had a substantial cation requirement. The enzyme solubilized from the lymphocyte therefore generally resembles fraction 2 of serum.
D002413:Cations, Divalent; D006801:Humans; D007700:Kinetics; D007945:Leukemia, Lymphoid / Q000201:enzymology*; D008214:Lymphocytes / Q000201:enzymology*; D012799:Sialyltransferases / Q000097:blood* / Q000302:isolation & purification; D014166:Transferases / Q000097:blood*
D002413:Cations, Divalent; D014166:Transferases; D012799:Sialyltransferases