Protein heterogeneity of lipoprotein particles containing apolipoprotein A-I without apolipoprotein A-II and apolipoprotein A-I with apolipoprotein A-II isolated from human plasma

Détails

ID Serval
serval:BIB_B097B94D9257
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Protein heterogeneity of lipoprotein particles containing apolipoprotein A-I without apolipoprotein A-II and apolipoprotein A-I with apolipoprotein A-II isolated from human plasma
Périodique
Journal of Lipid Research
Auteur(s)
James  R. W., Hochstrasser  D., Tissot  J. D., Funk  M., Appel  R., Barja  F., Pellegrini  C., Muller  A. F., Pometta  D.
ISSN
0022-2275 (Print)
Statut éditorial
Publié
Date de publication
12/1988
Volume
29
Numéro
12
Pages
1557-71
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Dec
Résumé
The protein heterogeneity of fractions isolated by immunoaffinity chromatography on anti-apolipoprotein A-I and anti-apolipoprotein A-II affinity columns was analyzed by high resolution two-dimensional gel electrophoresis. The two-dimensional gel electrophoresis profiles of the fractions were analyzed and automatically compared by the computer system MELANIE. Fractions containing apolipoproteins A-I + A-II and only A-I as the major protein components have been isolated from plasma and from high density lipoproteins prepared by ultracentrifugation. Similarities between the profiles of the fractions, as indicated by two-dimensional gel electrophoresis, suggested that those derived from plasma were equivalent to those from high density lipoproteins (HDL), which are particulate in nature. The established apolipoproteins (A-I, A-II, A-IV, C, D, and E) were visible and enriched in fractions from both plasma and HDL. However, plasma-derived fractions showed a much greater degree of protein heterogeneity due largely to enrichment in bands corresponding to six additional proteins. They were present in trace amounts in fractions isolated from HDL and certain of the proteins were visible in two-dimensional gel electrophoresis profiles of the plasma. These proteins are considered to be specifically associated with the immunoaffinity-isolated particles. They have been characterized in terms of Mr and pI. Computer-assisted measurements of protein spot-staining intensities suggest an asymmetric distribution of the proteins (as well as the established apolipoproteins), with four showing greater prominence in particles containing apolipoprotein A-I but no apolipoprotein A-II.
Mots-clé
Apolipoprotein A-I Apolipoprotein A-II Apolipoproteins A/*blood/isolation & purification Chemical Fractionation Chromatography, Affinity Electrophoresis, Gel, Two-Dimensional Humans Immunosorbents Isoelectric Point Lipoproteins, HDL/*blood Male Molecular Weight
Pubmed
Web of science
Création de la notice
25/01/2008 15:34
Dernière modification de la notice
20/08/2019 15:19
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