Fluorescence anisotropy decay studies upon hemoglobin A and its subunits
Fluorescence anisotropy decay studies upon hemoglobin A and its subunits
复制标题
血红蛋白A及其亚基的荧光各向异性衰减研究
DOI：
10.1002/bip.1979.360180516
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发表时间：
1979
期刊：
影响因子：
2.9
通讯作者：
R. Steiner
中科院分区：
文献类型：
--
作者：
E. Bucci;C. Fronticelli;K. Flanigan;J. Perlman;R. Steiner
制备了血红蛋白A、其分离的β链和β链的载脂蛋白衍生物的荧光缀合物，其中β-93巯基与1，5-AEDANS缀合。无辐射能量转移到血红素基团导致荧光强度和衰减时间大幅下降。采用单光子计数的荧光各向异性的时间衰减的测量表明，在每种情况下，表观旋转相关时间从相同分子量的刚性分子的预期值大幅降低。这一观察提出了内部旋转自由度存在的可能性。
Fluorescent conjugates of hemoglobin A, its isolated β‐chain, and the apo‐derivative of the β‐chain have been prepared in which the β‐93 sulfhydryl was conjugated with 1,5‐AEDANS. Radiationless enery transfer to the heme group results in a major decrease in fluorescence intensity and decay time. Measurements of the time decay of fluorescence anisotropy, employing single‐photon counting, indicate that the apparent rotational correlation time is, in each case, substantially reduced from the value expected for a rigid molecule of the same molecular weight. This observation raises the possibility that internal degrees of rotational freedom exist.