ON THE GEOMETRICAL ARRANGEMENT OF THE PROTEIN SUBUNITS OF HUMAN SERUM LOW-DENSITY LIPOPROTEIN: EVIDENCE FOR A DODECAHEDRAL MODEL*
AUTOR(ES)
Pollard, H.
RESUMO
Ultracentrifugal and electron microscopic studies of human serum low-density lipoprotein (LDL) and several of its derivatives led to the formulation of a model in which the 20 protein subunits, probably globular, are arranged in a dodecahedral pattern with icosahedral symmetry. In such a model the LDL surface is occupied by both protein and lipids, predominantly phospholipids, as supported by the results of the hydrolysis of LDL by phospholipase A and C. Neutral lipids (cholesterol esters and glycerides) would be in the interior of the molecule.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=286162Documentos Relacionados
- ON THE CONFORMATIONAL INSTABILITY OF HUMAN SERUM LOW-DENSITY LIPOPROTEIN: EFFECT OF TEMPERATURE*
- REVERSIBLE THERMAL CONFORMATION CHANGES IN HUMAN SERUM LOW-DENSITY LIPOPROTEIN*
- Development of Capture Assays for Different Modifications of Human Low-Density Lipoprotein
- High-density lipoprotein, low-density lipoprotein, and coronary heart disease.
- Low-density lipoprotein oxidation and the pathogenesis of atherosclerosis.
