原卟啉与血红素结合蛋白及白蛋白结合的荧光研究。
Fluorimetric study of the binding of protoporphyrin to haemopexin and albumin.
作者信息
Lamola A A, Asher I, Muller-Eberhard U, Poh-Fitzpatrick M
出版信息
Biochem J. 1981 Jun 15;196(3):693-8. doi: 10.1042/bj1960693.
Abstract
Fluorescence spectra of protoporphyrin bound to its most affinitive site on human serum albumin, bound to human haemopexin and dissolved in human plasma reveal that, when present in plasma, at least 90% of this porphyrin is bound to albumin. Human serum albumin binds protoporphyrin with an affinity KA = 3 X 10(9)M-1 in phosphate-buffered saline. The affinity of haemopexin for protoporphyrin is 4 times smaller. From these data it is concluded that less than 1% of plasma protoporphyrin is bound to haemopexin. Implications of the data for protoporphyrin transport and clearance are discussed.
摘要
与人类血清白蛋白上最具亲和力的位点结合、与人类血红素结合蛋白结合并溶解于人类血浆中的原卟啉的荧光光谱显示，当存在于血浆中时，这种卟啉至少90%与白蛋白结合。在磷酸盐缓冲盐水中，人类血清白蛋白与原卟啉的结合亲和力KA = 3×10⁹M⁻¹。血红素结合蛋白对原卟啉的亲和力小4倍。根据这些数据得出结论，血浆中原卟啉与血红素结合蛋白结合的比例不到1%。讨论了这些数据对原卟啉转运和清除的意义。
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