Structural variety and biological function of apolipoprotein H (.BETA.2-glycoprotein I).
スポンサーリンク
概要
- 論文の詳細を見る
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.
- 日本電気泳動学会の論文
日本電気泳動学会 | 論文
- Multiple reaction monitoring をバリデーションに用いた質量分析による血漿バイオマーカー探索システムの検討
- リポソームをリガンドとして用いた血漿蛋白質のプロテオミクス解析
- 白血球DNAの分析と症例
- キャピラリー電気泳動およびDHPLCによる遺伝子解析法
- 骨髄由来細胞動員を介した組織再生制御機構