Purification of the human anionic polypeptide fraction of the apo‐bile lipoprotein complex by zonal ultracentrifugation

Purification of the human anionic polypeptide fraction of the apo‐bile lipoprotein complex by zonal ultracentrifugation

The two main proteic constituents of the human Apo‐bile lipoprotein complex (BLC), i.e., the anionic polypeptide fraction (APF) and the IgA fragments, were separated by preparative zonal ultracentrifugation using a sucrose gradient containing 1.5 mM glycodesoxycholate. The purification of the APF wa...

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Veröffentlicht in:Lipids 1985-12, Vol.20 (12), p.884-889
Hauptverfasser: Martigne, M., Domingo, N., Lafont, H., Nalbone, G., Hauton, J. C.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acids - analysis
Analysis of complex biological substances
Analytical, structural and metabolic biochemistry
Apolipoproteins - isolation & purification
Bile - analysis
Biological and medical sciences
Blood and biological fluids
Centrifugation, Zonal - methods
Fundamental and applied biological sciences. Psychology
Humans
Immune Sera
Immunodiffusion
Molecular Weight
Peptides - isolation & purification
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Zusammenfassung:The two main proteic constituents of the human Apo‐bile lipoprotein complex (BLC), i.e., the anionic polypeptide fraction (APF) and the IgA fragments, were separated by preparative zonal ultracentrifugation using a sucrose gradient containing 1.5 mM glycodesoxycholate. The purification of the APF was verified by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis and immunology, and its amino acid composition then was determined. This procedure was used to obtain a polyclonal antiserum directed solely against the APF.
ISSN:0024-4201
1558-9307
DOI:10.1007/BF02534772