The binding of apolipoprotein H (beta2-Glycoprotein I) to lipoproteins.
Beta2-glycoprotein I has a high affinity for triglyceride-rich particles, activates lipoprotein lipase, and is also defined as an apolipoprotein H. Previous studies have shown that apolipoprotein H is a regular structural component of the major classes of lipoproteins. In view of these findings, we analyzed the interactions of apolipoprotein H with lipoproteins in the fasting plasma of eight normal, seven hypertriglyceridemic, and seven hypercholesterolemic subjects. After rate-zonal, density gradient ultracentrifugation, apolipoprotein H was little distributed among the different density fractions, and most of it was recovered in the last fraction that contained the lipoprotein-free plasma. A small percentage (4-13%) of the apolipoprotein H associated with plasma lipoproteins was detected at the density ranging from 1.090 to 1.225 g/ml. This result means that apolipoprotein H is little associated with lipoproteins.
Gambino
R
R
Dipartimento di Medicina Interna, Universitá di Torino, Italy.
Ruiu
G
G
Pagano
G
G
Cassader
M
M
D016022:Case-Control Studies; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D006937:Hypercholesterolemia / Q000097:blood; D015228:Hypertriglyceridemia / Q000097:blood; D008074:Lipoproteins / Q000097:blood*; D011485:Protein Binding; D014461:Ultracentrifugation; D053482:beta 2-Glycoprotein I
D006023:Glycoproteins; D008074:Lipoproteins; D053482:beta 2-Glycoprotein I