Cierniewski C S, Babińska A, Koziołkiewicz W, Wasiak T
Hoppe Seylers Z Physiol Chem. 1984 Apr;365(4):499-502. doi: 10.1515/bchm2.1984.365.1.499.
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.
合成片段和类似物被用于表征抗P物质抗血清的特异性。C末端六肽和五肽均能完全抑制这些抗血清对125I-[酪氨酸8]P物质的结合，表明它们与P物质具有抗原同一性。比肽（7-11）短的合成片段在该系统中不与抗P物质抗血清发生反应。在片段（6-11）或（7-11）的不同位置用组氨酸或甘氨酸取代氨基酸，结果显示所有五个氨基酸残基均参与抗原决定簇的结构。
