Some properties of sialyltransferase in plasma and lymphocytes of patients with chronic lymphocytic leukemia

Eur J Biochem. 1978 Jan 16;82(2):535-41. doi: 10.1111/j.1432-1033.1978.tb12048.x.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cations, Divalent
  • Humans
  • Kinetics
  • Leukemia, Lymphoid / enzymology*
  • Lymphocytes / enzymology*
  • Sialyltransferases / blood*
  • Sialyltransferases / isolation & purification
  • Transferases / blood*

Substances

  • Cations, Divalent
  • Transferases
  • Sialyltransferases