Collagen polymorphism in mature rabbit cornea.
Collagen polymorphism in mature rabbit cornea.
复制标题
成熟兔角膜中胶原蛋白多态性。
DOI：
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发表时间：
1978
影响因子：
4.4
通讯作者：
I. Freeman
中科院分区：
文献类型：
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作者：
I. Freeman
用 NaCl-Tris 缓冲液和乙酸连续提取成熟的兔角膜基质仅溶解了总角膜胶原的 12%。 0.4 M 乙酸中的胃蛋白酶（E:S 1:10，4 摄氏度，48 小时）溶解了残留物中总胶原蛋白的 91% 至 95%。大约 68% 的溶解物质可以在 2.5M NaCl 下沉淀，另外 3% 至 9% 在 3.5M NaCl 下沉淀。在 2.5M NaCl 下沉淀的胶原材料含有 α、β、γ 和一些较高分子量的成分，并且具有与牛 I 型皮肤胶原相似的 CNBr 特征。它的羟基赖氨酸/赖氨酸 (OHLys/Lys) 比率为 0.43，与皮肤胶原蛋白相似，但与皮肤胶原蛋白不同的是，它的糖基化率为 52%。尽管 3.5M NaCl 沉淀物具有与 I 型胶原相似的 CNBr 肽谱，但它含有两条额外的胶原链，分子量分别约为 140,000 和 100,000 道尔顿，OHLys/Lys 比率为 0.62，并且糖基化率为 66%。通过凝胶电泳从胶原蛋白沉淀物中分离出单独的链，并且额外的胶原蛋白链显示出富含碳水化合物。这些额外的胶原链可以源自一种或多种分子种类，这些分子种类对于维持角膜胶原的独特组织具有生理上重要的作用。
Sequential extraction of mature rabbit corneal stroma with NaCl-Tris buffer and acetic acid solubilized only 12% of the total corneal collagen. Pepsin (E:S 1:10,4 degrees C, 48 hr) in 0.4 M acetic acid solubilized 91% to 95% of the total collagen in the residue. Approximately 68% of the solubilized material could be precipitated at 2.5M NaCl and a further 3% to 9% at 3.5M NaCl. The collagenous material precipitating at 2.5M NaCl contained alpha, beta, gamma, and some higher molecular weight components and had a CNBr profile similar to bovine type I skin collagen. It had an hydroxylysine/lysine (OHLys/Lys) ratio of 0.43, similar to that of skin collagen, but unlike skin collagen was 52% glycosyled. Although the 3.5M NaCl precipitate had a CNBr peptide profile similar to that of type I collagen, it contained two additional collagen chains of molecular weight approximately 140,000 and 100,000 daltons, had an OHLys/Lys ratio of 0.62, and was 66% glycosylated. Individual chains were separated from the collagen precipitates by gel electrophoresis,and the additional collagen chains were shown to be carbohydrate rich. These additional collagen chains may be derived from one or more molecular species which are physiologically important in the maintenance of the unique organization of corneal collagen.