Receptor-mediated internalization of tuftsin by human polymorphonuclear leukocytes.

A A Amoscato, P J Davies, G F Babcock, K Nishioka
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Abstract

A high-performance liquid chromatography (HPLC) purified fluorescein-labeled analogue of tuftsin was prepared, which retains the full biological activity of the native molecule. Characterization of the derivatization site by amino acid analysis, N-terminal cleavage, and dansylation revealed a monofluorescinated derivative at the alpha-amino terminus. Binding of the fluorescent tuftsin to living polymorphonuclear leukocytes (PMN) was observed by means of video intensification microscopy. At 37 degrees C, diffuse membrane fluorescence was seen initially, followed by rapid aggregation and internalization. The latter was demonstrated by saltation of intracellular fluorescent aggregates. These processes are temperature-dependent and rely on specific binding to the tuftsin receptor.

受体介导的人多形核白细胞的内化。
制备了一种高效液相色谱(HPLC)纯化的荧光素标记的簇毛素类似物,它保留了天然分子的全部生物活性。通过氨基酸分析、n端裂解和丹酰化对衍生化位点进行表征,发现在α -氨基端有一个单荧光衍生物。通过视频增强显微镜观察荧光簇与活的多形核白细胞(PMN)的结合。在37℃时,最初可见弥漫性膜荧光,随后迅速聚集和内化。后者通过细胞内荧光聚集体的跳跃来证明。这些过程是温度依赖性的,并且依赖于对簇状蛋白受体的特异性结合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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