Migliorini M G, Galvan P, Sbrana G, Donzelli G P, Vecchi C
Dipartimento di Chimica, Università di Firenze, Italy.
Biochem J. 1988 Dec 15;256(3):841-6. doi: 10.1042/bj2560841.
Structural and geometric photoisomerization of bilirubin bound to human serum albumin was investigated. Solutions were irradiated with monochromatic light emitted by an Ar ion laser, the 457.9, 488.0 and 514.5 nm wavelengths being selected. Photoproducts were separated and analysed by h.p.l.c. Visible-absorption spectra of pure ZZ-bilirubin, ZE-bilirubin and lumirubin in the eluent were registered in the 350-550 nm region by collecting single fractions by h.p.l.c. Wavelength-dependence of bilirubin photoconversion was studied within photoequilibrium and up to a large decrement of the total concentration. Experiments were performed in aerobic and anaerobic conditions in order to assess the contribution of the photo-oxidation to the overall process. The presence of O2 was found to increase the rate of bilirubin degradation and unexpectedly to favour lumirubin production. The ability of 514.5 nm irradiation to induce bilirubin cyclization was definitively confirmed.
研究了与人类血清白蛋白结合的胆红素的结构和几何光异构化。用氩离子激光发射的单色光照射溶液,选择457.9、488.0和514.5 nm波长。通过高效液相色谱法分离和分析光产物。通过高效液相色谱法收集单个馏分,在350 - 550 nm区域记录洗脱液中纯ZZ-胆红素、ZE-胆红素和光胆红素的可见吸收光谱。在光平衡范围内以及总浓度大幅降低之前,研究了胆红素光转化的波长依赖性。在有氧和无氧条件下进行实验,以评估光氧化对整个过程的贡献。发现氧气的存在会增加胆红素的降解速率,并且出乎意料地有利于光胆红素的产生。最终证实了514.5 nm照射诱导胆红素环化的能力。