Covalent Binding of Photosensitive 1-(12-Azido-[9,10-3H2]oleoyl)glycero-3-phosphocholine (Lysolecithin) to Human Serum High Density Apolipoproteins
- 1 January 1979
- journal article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 360 (2) , 1319-1326
- https://doi.org/10.1515/bchm2.1979.360.2.1319
Abstract
Human serum high density apoproteins were complexed with increasing concentrations of 1-(12-azido-[9,10(-3)H2]oleoyl)glycero-3-phosphocholine up to the saturation concentration (72 mol lysolecithin per mol apo HDL). Ultraviolet irradiation generated the nitrene which led to crosslinking with the two main apolipoproteins AI and AII. Methods are described for the removal of excess, unbound lipid and the column chromatographic separation of the lipopolypeptides AI and AII.Keywords
This publication has 5 references indexed in Scilit:
- Covalent Cross-linking of Photosensitive Phospholipids to Human Serum High Density Apolipoproteins (apoHDL)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Lipid-Protein Interactions between Human Apolipoprotein A-I and Defined Sphingomyelin Species. A13C-NMR Spectroscopic StudyHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1977
- Studies of the lipid binding characteristics of the apolipoproteins from human high density lipoproteinBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1976
- Human High Density Apolipoprotein A-I-Lysolecithin-Lecithin and Sphingomyelin Complexes. A Method for High Yield Recombinations to Lipoprotein Complexes of Reproducible StoichiometryHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- A new method for isolating the nonidentical protein subunits of human plasma α-lipoproteinJournal of Clinical Investigation, 1970