FLUORESCENCE AND STRUCTURE OF PROTEINS .4. IODINATED TYROSYL RESIDUES
FLUORESCENCE AND STRUCTURE OF PROTEINS .4. IODINATED TYROSYL RESIDUES
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DOI：
10.1016/0926-6585(65)90009-9
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发表时间：
1965-01-01
期刊：
影响因子：
--
通讯作者：
COWGILL, RW
中科院分区：
文献类型：
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作者：
COWGILL, RW
酪氨酸、Tyr-Tyr、胰岛素和核糖核酸酶在酚环碘化后荧光发生变化。荧光损失似乎有两个来源。一是被碘化的酪氨酰残基完全丧失；第二个是由于激发能量转移到碘酪氨酰残基而导致非碘化酪氨酰残基的荧光部分损失。导出了用于评估碘酪氨酰残基作为能量汇的效率的方程。部分碘化Tyr-Tyr和核糖核酸酶的荧光滴定曲线表明这些化合物中碘酪氨酰残基的吸收效率对碘酪氨酰残基的电离状态不敏感。
Changes in fluorescence upon iodination of the phenolic rings were followed for tyrosine, Tyr-Tyr, insulin and ribonuclease. Losses of fluorescence appear to arise from two sources. One is the complete loss from the tyrosyl residues that were iodinated; the second is the partial loss of fluorescence of non-iodinated tyrosyl residues by transfer of excitation energy to the iodotyrosyl residues. Equations were derived for evaluation of the efficiency of iodotyrosyl residues as energy sinks. Fluorimetric titration curves of partially iodinated Tyr-Tyr and ribonuclease indicate that the sink efficiency of iodotyrosyl residues in these compounds is not sensitive to the ionization state of the iodo tyrosyl residues.