P物质合成片段和类似物的免疫化学分析。

C S Cierniewski, A Babińska, W Koziołkiewicz, T Wasiak
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引用次数: 2

摘要

用合成片段和类似物表征了抗血清对P物质的特异性。c端六肽和五肽完全抑制了这些抗血清对125I-[Tyr8] P物质的结合,显示了与P物质的抗原同源性。用组氨酸或甘氨酸取代片段(6-11)或(7-11)中不同位置的氨基酸表明,这5个氨基酸残基都参与了抗原决定因子的一个结构。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Immunochemical analysis of substance P using its synthetic fragments and analogs.

Synthetic fragments and analogs were used to characterize specificity of antisera to substance P. Both, the C-terminal hexapeptide and the pentapeptide completely inhibited binding of 125I-[Tyr8]substance P by these antisera, showing the antigenic identity with substance P. Synthetic fragments shorter than peptide (7-11) did not react with anti-substance P antisera in this system. Substitution of amino acids in different positions in the fragments (6-11) or (7-11) by histidine or glycine revealed that all five amino-acid residues take part in a structure of the antigenic determinant.

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