<原著>デルタビリルビンにおけるビリルビン・アルブミン共有結合部位の検討
スポンサーリンク
概要
- 論文の詳細を見る
Delta bilirubin (Bδ) is a covalently albumin-bound bilirubin. A bilirubin binding amino acid residue of human albumin was identified using a large amount of B8 fraction prepared from pooled icteric human serum. Bilirubin in pooled icteric human serum was first changed to an azoderivative by the addition of a diazo reagent to protect it from degradation. The azoderivative of B8 (azoB8) was prepared by affinity chromatography and high performance liquid chromatography (HPLC) using a preparative Micronex RP30 column. The BrCN-treated azo Bδ was digested with Achromobacter protease I and with Staphylococcal serine proteinase, sequentially. The fragmented peptides were fractionated by reversed phase HPLC using a μBondasphere column. A fraction which showed absorbance reaks both at 530 nm and at 215 nm was obtained and analyzed by a protein/peptide sequencer and an analyzer. The finally obtained peptide fraction was composed of amino acid residues 18 to 38 of human serum albumin. The detected molar amount of lysine 20 was about one third of that of the other amino acids which suggested the covalent bonding of bilirubin to lysine 20 of human serum albumin.
- 近畿大学の論文
- 1993-03-25