Starcher B, Cook G, Gallop P, Hensen E, Shoulders B
Connect Tissue Res. 1987;16(1):15-25. doi: 10.3109/03008208709001991.
An unknown amino acid was purified from bovine ligament elastin. The compound was shown by proton NMR to have a pyridinium ring structure similar to isodesmosine, yet containing an olefinic double bond on one additional side chain which was not attached to the pyridinium ring. Mass spectral analysis confirmed the NMR data and indicated a parent compound with a mass of 653. A structure is proposed that is derived from the condensation of five lysine residues. The trivial name of pentasine is proposed for this compound.
从牛韧带弹性蛋白中纯化出一种未知氨基酸。通过质子核磁共振（NMR）表明该化合物具有与异锁链素相似的吡啶鎓环结构，但在一个未连接到吡啶鎓环的额外侧链上含有一个烯键式双键。质谱分析证实了核磁共振数据，并表明母体化合物的质量为653。提出了一种由五个赖氨酸残基缩合衍生而来的结构。为此化合物提议使用俗名五聚赖氨酸。
