Studies on the serum amyloid A (SAA) protein. Purification, physicochemical and immunochemical properties.:Purification, physicochemical and immunochemical properties
スポンサーリンク
概要
- 論文の詳細を見る
SAA (serum amyloid A) protein was isolated from plasma of patients with active phase of rheumatoid arthritis. It's purification steps involved sequential ultracentrifugation, delipidation with organic solvent, gel filtration on Sephadex G-200 in the presence of 6M urea, rechromatography on same column and immunoaffinity chromatography. The purity of this protein was checked by SDS-PAGE, N-terminal amino acid sequence and immunochemical analysis. The molecular weight of this protein was 12, 000 daltons by SDS-PAGE (with or without reducing agent) and showed 4 bands on analytical isoelectric focusing. N-terminal amino acid sequence was NH2-S·F·F·S·F·L·G·E·A·F·D·G·A·R·D·M·W·R·A·Y·· and Amino acid composition agreed with the previous report. Antiserum against purified SAA was produced in rabbit. Immunological properties of the antiserum were characterised.
- 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