Suyama K, Nakamura F
Molecular Technology of Animal Products, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Biochem Biophys Res Commun. 1990 Jul 31;170(2):713-8. doi: 10.1016/0006-291x(90)92149-t.
A new pentafunctional cross-linking amino acid, termed allodesmosine, was isolated from bovine ligamentum nuchae elastin. This compound was a very hygroscopic, white amorphous solid with a faint yellow tinge, soluble in aqueous solvents but not dry methanol; it was characterized by UV, FAB mass and NMR spectroscopy. The compound was shown by UV and 1H-NMR to have a pyridinium ring structure similar to desmosine. Mass spectral analysis indicated a parent compound with a mass of 655. We postulated that it arose by condensation of a reduced aldol condensation product of allysine, allysine and lysine.
一种新的五功能交联氨基酸，称为别锁链素，是从牛项韧带弹性蛋白中分离出来的。该化合物是一种极易吸湿的白色无定形固体，略带淡黄色，可溶于水性溶剂，但不溶于无水甲醇；通过紫外光谱、快原子轰击质谱和核磁共振光谱对其进行了表征。紫外光谱和¹H-NMR表明该化合物具有与锁链素相似的吡啶环结构。质谱分析表明母体化合物的分子量为655。我们推测它是由烯赖氨酸、烯赖氨酸和赖氨酸的还原羟醛缩合产物缩合而成的。
