Studies on the pre-alpha-lipoprotein in patients with familial lecithin: cholesterol acyltransferase deficiency.

Abstract

The present study shows that regular alpha1- and pre-alpha-lipoproteins cannot be detected in serum of patients with familial lecithin: cholesterol acyltransferase (LCAT) deficiency. After electrophoresis on agarose gel only one single band of albumin mobility was observed in the alpha1-pre-alpha-region. In contrast to sera of normal subjects neither the anodic front nor the cathodic part of this region revealed any lipoprotein bands in the patients studied. The lack of the cathodic part might be related to a low amount of alpha1-lipoprotein. The apparent lack of the anodic front could be related to a low amount of "albumin-Apo-A-I-containing lipoprotein" (AAL). AAL was not detected with conventional methods in LCAT deficient sera. The alpha1-lipoprotein was made up of two immunologically identical peaks, both of which had a Sudanophilic character. After incubation of lysolecithin with albumin and AAL and subsequent thin layer chromatography, a significant lysolecithin-binding capacity of AAL was demonstrated, superior to that possessed by albumin.

• Authors: L E Wille, H Torsvik, E Gjone
• Journal: Clinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 77 Issue 3 Pg. 423-9 (Jun 15 1977) ISSN: 0009-8981 [Print] Netherlands
• PMID: 194737 (Publication Type: Journal Article)

Chemical References

• Apolipoproteins
• Lipoproteins, HDL
• Lysophosphatidylcholines
• Serum Albumin
• Acyltransferases

Topics

• Acyltransferases (deficiency)
• Apolipoproteins (blood)
• Blood Protein Electrophoresis
• Electrophoresis, Agar Gel
• Female
• Humans
• Immunoelectrophoresis, Two-Dimensional
• Lecithin Cholesterol Acyltransferase Deficiency
• Lipid Metabolism, Inborn Errors (blood, genetics)
• Lipoproteins, HDL (blood)
• Lysophosphatidylcholines (blood)
• Male
• Protein Binding
• Serum Albumin (analysis)