1994 Volume 38 Issue 1 Pages 1-5
Structural property of apolipoprotein H (β2-glycoprotein I) (apo H) was analyzed by two-dimensional electrophoresis and two-dimensional immunoblotting. Untreated purified apo H could be separated into six spots of molecular size (M=49, 000) in two-dimensional electrophoresis at pI 5-7. Spot number was decreased and size of apo H was reduced by neuraminidase treatment to three spots of molecular size 48, 000. These results suggested that structural variety of apo H was concerned partly to glycosilation of the protein. We also found that purified apo H of pooled serum from patients with hyperlipidemia has hemolytic ability to human red blood cell.
