[α1(III)]3 Human Skin Collagen RELEASE BY PEPSIN DIGESTION AND PREPONDERANCE IN FETAL LIFE
[α1(III)]3 Human Skin Collagen RELEASE BY PEPSIN DIGESTION AND PREPONDERANCE IN FETAL LIFE
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[α1(III)]3 胃蛋白酶消化引起的人皮肤胶原蛋白释放及其在胎儿生命中的优势
DOI：
10.1016/s0021-9258(19)42661-6
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发表时间：
1974
影响因子：
4.8
通讯作者：
E. Epstein
中科院分区：
文献类型：
--
作者：
E. Epstein
人真皮在保持大量胶原蛋白螺旋构象的条件下，用胃酶消化。在pH 7.5条件下，用差示盐析的方法从[α1(I)]2α2胶原蛋白中分离出含有α1(III)链的分子，并利用α裂解产生的多肽监测各组分的组成，分离出的分子由3个CNB 1(III)链组成，这些链通过二硫键交联。暴露于二硫苏糖醇可以释放这三条明显相同的链，这些链被洗脱到位于α1(I)和α2中间位置的羧甲基纤维素层析上。这些链的胃蛋白酶抗性部分与先前分离的胶原链的大小相同。人真皮也用氰基溴消化，得到的α1(I)和α1(III)肽被层析分离。这些多肽的相对数量表明，α1(III)链在早期胎儿皮肤中占主导地位，但在出生后和以后的生活中，α1(I)链的数量大约是胎儿的3倍。
Human dermis was digested with pepsin under conditions that maintain the helical conformation of the bulk of the collagen. Molecules containing α1(III) chains were separated from [α1(I)]2α2 collagen by differential salt precipitation at pH 7.5, with the use of the peptides produced by CNBr cleavage to monitor the composition of each fraction.The isolated molecules are composed of three α1(III) chains, and these chains are cross-linked by disulfide bonds. Exposure to dithiothreitol liberates the three apparently identical chains, and these elute on carboxymethylcellulose chromatography at a position intermediate between α1(I) and α2. The pepsin-resistant portion of these chains is the same size as that of previously isolated collagen chains.Human dermis was also digested with CNBr, and resultant α1(I) and α1(III) peptides were separated chromatographically. The relative quantities of these peptides indicate that α1(III) chains predominate in early fetal skin, but by birth and in later life α1(I) chains are approximately 3 times as plentiful.