Noguchi M, Yoshida T, Kikuchi G
J Biochem. 1982 May;91(5):1479-83. doi: 10.1093/oxfordjournals.jbchem.a133839.
Biliverdins formed from heme by a microsomal preparation and a reconstituted heme oxygenase system were each converted to their dimethyl esters and analyzed for isomeric composition by reversed-phase high-performance liquid chromatography, using a column of mu Bondapak C18 (Waters Associates); on this column, the dimethyl esters of four biliverdin IX isomers, that is IX alpha, IX beta, IX gamma, and IX delta, have been shown to be eluted separately in the order IX alpha, IX beta, IX delta, and IX gamma, when developed with methanol/water. The analysis indicated that the enzymatically formed biliverdins were exclusively IX alpha; the elution profile exhibited no other significant elution peak due to other biliverdin isomers. It was concluded that the heme oxygenase system cleaves the heme ring specifically at the alpha-methene bridge to yield biliverdin IX alpha.
由微粒体制剂和重组血红素加氧酶系统从血红素形成的胆绿素分别转化为它们的二甲酯，并通过反相高效液相色谱法分析其异构体组成，使用μ Bondapak C18柱（沃特世公司）；在该柱上，四种胆绿素IX异构体，即IXα、IXβ、IXγ和IXδ的二甲酯，在用甲醇/水展开时，已显示按IXα、IXβ、IXδ和IXγ的顺序分别洗脱。分析表明，酶促形成的胆绿素仅为IXα；洗脱图谱未显示由于其他胆绿素异构体产生的其他明显洗脱峰。得出的结论是，血红素加氧酶系统在α-次甲基桥处特异性切割血红素环，产生胆绿素IXα。
