Intrinsic fluorometric determination of the stable state of aggregation in hemoglobins.
Intrinsic fluorometric determination of the stable state of aggregation in hemoglobins.
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DOI：
10.1016/0003-2697(85)90592-5
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发表时间：
1985-09
影响因子：
2.9
通讯作者：
R. E. Hirsch;R. C. San George;R. Nagel
中科院分区：
文献类型：
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作者：
R. E. Hirsch;R. C. San George;R. Nagel
正面荧光法可以检测血红蛋白（R。e.赫希河S. Zukin和R. L.内格尔，1980，生物化学和生物物理。Res. Commun.，93，432 - 439），这是一种可用于研究人血红蛋白（R. e. Hirsch，N. a.斯奎尔斯角Discepola，和R. L.内格尔，1983，生物化学和生物物理。Res. Commun.，116，712 - 718）。我们报告说，稳定的二聚体血红蛋白成分的arcid蛤Noetia ponderosa和Anadara椭圆形的荧光发射最大值转移到更长的波长相比，四聚体的人血红蛋白。相反，A.卵圆形的显示出与四聚体HbA相似的发射最大值。因此，稳定的二聚体血红蛋白可以通过相对于Hb A在更长波长处的发射最大值来检测。配体结合这些蛤血红蛋白的荧光研究表明，这些成分之间的结构和功能的差异，并与血红蛋白A。我们的结论是，不同的稳定聚集状态的血红蛋白可以确定由固有荧光时，研究与正面光学。
Front-face fluorometry can detect steady-state intrinsic fluorescence of hemoglobins (R. E. Hirsch, R. S. Zukin, and R. L. Nagel, 1980, Biochem. Biophys. Res. Commun., 93, 432–439), a property that can be used to study the dimerization of human hemoglobins (R. E. Hirsch, N. A. Squires, C. Discepola, and R. L. Nagel, 1983, Biochem. Biophys. Res. Commun., 116, 712–718). We report that the stable dimeric hemoglobin components of the arcid clams Noetia ponderosa and Anadara ovalis exhibit fluorescence emission maxima shifted to longer wavelengths compared to tetrameric human hemoglobin. Conversely, the tetrameric major hemoglobin (Hb) component of A. ovalis exhibits an emission maximum similar to that of tetrameric Hb A. Hence, stable dimeric hemoglobins can be detected by emission maxima at longer wavelengths relative to Hb A. Fluorescence studies of ligand binding to these clam hemoglobins indicate structural and functional differences among these components and compared to Hb A. We conclude that different stable aggregation states of hemoglobins may be determined by intrinsic fluorescence when studied with front-face optics.