Human plasma lecithin-cholesterol acyltransferase. The vicinal nature of cysteine 31 and cysteine 184 in the catalytic site.

This publication has 38 references indexed in Scilit:

• The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theory
  Published by Elsevier ,2003
• Aromatic boronic acids as probes of the catalytic site of human plasma lecithin—cholesterol acyltransferase
  Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1987
• The catalytic center of lecithin: Cholesterol acyltransferase: Isolation and sequence of diisopropyl fluorophosphate-labeled peptides
  Biochemical and Biophysical Research Communications, 1987
• Further characterization of purified lecithin:Cholesterol acyltransferase from human plasma
  Biochemical Medicine, 1981
• Organic extraction and preparative isoelectric focussing of rat serum apolipoproteins
  FEBS Letters, 1980
• Crystal structure of the β-form of tetra-arsenic trisulphide
  J. Chem. Soc., Dalton Trans., 1973
• Crystal and molecular structure of tetra-arsenic pentasulphide
  J. Chem. Soc., Dalton Trans., 1973
• Lecithin : Cholesterol acyltransferase : Effects of substrate composition upon enzyme activity
  Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1972
• The mechanism of the plasma cholesterol esterification reaction: Plasma fatty acid transferase
  Biochimica et Biophysica Acta, 1962
• The Determination of Enzyme Dissociation Constants
  Journal of the American Chemical Society, 1934