N-(1-芘基)碘乙酰胺标记f -肌动蛋白的荧光学研究。肌动蛋白原聚体在聚合和重肌球蛋白结合过程中的局部结构变化。

T. Kouyama, K. Mihashi
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引用次数: 746

摘要

将荧光试剂N-(1-芘基)碘乙酰胺偶联至兔骨骼肌肌动蛋白最活泼的巯基位点,研究了该偶联物的荧光特性(激发和发射光谱、量子产率、寿命)。与标记的g -肌动蛋白聚合有关,在365nm激发后,407nm处的荧光强度增强了约25倍。与重质肌凝蛋白(或亚片段1)结合后,其含量降低到25%左右。结果表明,重质肌凝蛋白与F-actin原聚体的结合使原聚体的局部结构向g -actin样结构转变。
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Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin.
A fluorescent reagent, N-(1-pyrenyl)iodoacetamide, was conjugated to rabbit skeletal muscle actin at the site of the most reactive sulfhydryl group, and fluorescence characteristics (excitation and emission spectra, quantum yields, lifetimes) of the conjugate were investigated. Associated with polymerization of labelled G-actin, the fluorescence intensity at 407 nm, after excitation at 365 nm, was enhanced by a factor of about 25. It was reduced to about 25% on the binding of heavy meromyosin (or subfragment 1). The results suggest that binding of heavy meromyosin to the protomer of F-actin alters the local structure of the protomer towards a G-actin-like one.
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