Isolation and characterization of lecithin-cholesterol acyltransferase from hog plasma

Yong B. Park, Andras G. Lacko

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Abstract

Lecithin-cholesterol acyltransferase (EC 2.3.1.43) was purified from hog plasma by a highly efficient procedure. The final enzyme preparation was purified 30000-fold over the starting material and was homogeneous as indicated by polyacrylamide gel electrophoreses in the presence of both SDS and urea. The purified hog lecithin-cholesterol acyltransferase had an apparent molecular weight of 66000 on SDS-poly-acrylamide gel electrophoresis and HPLC and was found to contain about 21.4% (w/w) carbohydrate-hexose, 11.3%; hexosamine, 1.9%; sialic acid, 8.2%. The amino acid composition analysis showed that hog lecithin-cholesterol acyltransferase contains four half cystines per mol; two cysteines were titrated at neutral pH with 5,5'-dithiobis(2-nitrobenzoic acid). Nearly all the phenolic groups were unavailable to the solvent at neutral pH, while they become exposed at around pH 11. Hog lecithin-cholesterol acyltransferase was found to be associated with HDL in the plasma and it prefers HDL as a substrate. The physicochemical properties of hog lecithin-cholesterol acyltransferase were generally similar to those of the human and the rat enzyme.

Original languageEnglish
Pages (from-to)179-190
Number of pages12
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume877
Issue number1
DOIs
StatePublished - 11 Jun 1986

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Keywords

  • (Porcine)
  • Amino acid composition
  • Enzyme purification
  • Lecithin-cholesterol acyltransferase

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