Henin-Pizieux O, Davril M, Han K K
Paroi Arterielle. 1979 Apr;5(1):41-53.
Normal and diseased human aortic elastins were isolated and highly purified. They were subsequently submitted to elastase and thermolysin digestion followed by partial acid hydrolysis to increase crosslinkage. The peptide fractions containing these highly cross-linked desmosines were extensively purified either by ion exchange chromatography or by gel-filtration. Their amino acid composition was determined. Detailed investigation of the purified peptide fraction from normal human elastin containing desmosines was carried out using different N-terminal and C-terminal procedures, thus permitting the probable covalent structure of the desmosine containing peptide(s) to be proposed. Irrespective of their origin (healthy or pathologic), the elastin samples all revealed the same amino acid composition with a very high alanine content in the cross-linking peptides. This work is submitted as proof that changes in amino acid composition are essentially due to "dilution" and contamination by structural glycoproteins and not to structural changes in amino acid compoistion in the vicinal cross-links positions. We find that not only "clustering" alanine residues but also glycine, proline, valine, leucine and tyrosine residues are located in the immediate vicinity of both desmosine and isodesmosine residues.
分离并高度纯化了正常和患病的人主动脉弹性蛋白。随后对它们进行弹性蛋白酶和嗜热菌蛋白酶消化，接着进行部分酸水解以增加交联。含有这些高度交联的锁链素的肽段通过离子交换色谱法或凝胶过滤法进行了广泛纯化。测定了它们的氨基酸组成。使用不同的N端和C端方法对来自正常人弹性蛋白且含有锁链素的纯化肽段进行了详细研究，从而提出了含锁链素肽段可能的共价结构。无论其来源（健康或患病）如何，弹性蛋白样品均显示出相同的氨基酸组成，交联肽中的丙氨酸含量非常高。这项工作旨在证明氨基酸组成的变化主要是由于结构糖蛋白的“稀释”和污染，而不是邻位交联位置氨基酸组成的结构变化。我们发现，不仅“聚集”的丙氨酸残基，而且甘氨酸、脯氨酸、缬氨酸、亮氨酸和酪氨酸残基都位于锁链素和异锁链素残基的紧邻位置。
