Intermolecular cross-linking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament.
Intermolecular cross-linking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament.
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DOI：
10.1021/bi00365a027
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发表时间：
1986-08
期刊：
影响因子：
2.9
通讯作者：
M. Yamauchi;E. P. Katz;E. P. Katz;G. Mechanic
中科院分区：
文献类型：
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作者：
M. Yamauchi;E. P. Katz;E. P. Katz;G. Mechanic
用胰蛋白酶消化变性NaB 3 H4还原的天然牛牙周膜，并通过凝胶过滤和纤维素离子交换柱层析进行分级。在胰蛋白酶消化之前，对完整的酸水解产物进行不可还原的稳定和可还原的分子间交联分析。微量的前者和显着量的减少交联二羟赖氨酸正亮氨酸（1.1摩尔/摩尔的胶原蛋白），羟赖氨酸正亮氨酸（0.9摩尔/摩尔的胶原蛋白），和histidinohydroxymerodesmosine（0.6摩尔/摩尔的胶原蛋白）被发现。不同的双链连接肽的结构是α 1CB 4 -5（76-90）[Hyl-87] X α 1CB 6-（993- 22 c）[Lysald-16 c]，α 1CB 4 -5（76-90）[Hyl-87] X α 1CB 6（993- 22 c）[Hylald-16 c]，α 2CB 4（76-90）[Hyl-87] X α 1CB 6（993- 22 c）[Lysald-16 c]，和α 2CB 4（76-90）[Hyl-87] X α 1CB 6（993- 22 c）[Hylald-16 c]。每个肽中的交联被糖基化。这是通过序列分析对胶原蛋白中α 2链中涉及Hyl-87的交联的第一次表征。在牛牙周膜中，Ⅰ型胶原分子的两条α 1链的羧基端非螺旋肽区中，16 c醛残基发生化学计量转化，形成分子间交联，α 1与α 2分子间交联链的比例为3.3：1，表明Ⅰ型胶原分子在牙周膜中存在立体定向的三维分子堆积。
A trypsin digest of denatured NaB3H4-reduced native bovine periodontal ligament was prepared and fractionated by gel filtration and cellulose ion-exchange column chromatography. Prior to trypsin digestion, a complete acid hydrolysate was subjected to analyses for nonreducible stable and reducible intermolecular cross-links. Minute amounts of the former and significant amounts of the reduced cross-links dihydroxylysinonorleucine (1.1 mol/mol of collagen), hydroxylysinonorleucine (0.9 mol/mol of collagen), and histidinohydroxymerodesmosine (0.6 mol/mol of collagen) were found. The covalent intermolecular cross-linked two-chained peptides that were isolated were subjected to amino acid and sequence analyses. The structures for the different two-chained linked peptides were alpha 1CB4-5(76-90)[Hyl-87] X alpha 1CB6-(993-22c)[Lysald-16c], alpha 1CB4-5(76-90)[Hyl-87] X alpha 1CB6(993-22c)[Hylald-16c], alpha 2CB4(76-90)[Hyl-87] X alpha 1CB6(993-22c)[Lysald-16c], and alpha 2CB4(76-90)[Hyl-87] X alpha 1CB6(993-22c)[Hylald-16c]. The cross-link in each peptide was glycosylated. This is the first characterization by sequence analysis of a cross-link involving Hyl-87 in an alpha 2 chain in collagen. A stoichiometric conversion of residue 16c aldehyde to an intermolecular cross-link in each of the COOH-terminal nonhelical peptide regions of both alpha 1 chains in a molecule of type I collagen was found. The ratio of alpha 1 to alpha 2 intermolecularly cross-linked chains involved was 3.3:1, indicating a stereospecific three-dimensional molecular packing of type I collagen molecules in bovine periodontal ligament.