ISOLATION OF A COLLAGEN FROM BASEMENT MEMBRANES CONTAINING 3 IDENTICAL ALPHA-CHAINS
ISOLATION OF A COLLAGEN FROM BASEMENT MEMBRANES CONTAINING 3 IDENTICAL ALPHA-CHAINS
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DOI：
10.1016/0006-291x(71)90073-8
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发表时间：
1971-01-01
影响因子：
3.1
通讯作者：
KEFALIDES, NA
中科院分区：
文献类型：
--
作者：
KEFALIDES, NA
从肾小球基底膜、透镜囊和后弹力膜分离的胶原的CM-纤维素的色谱研究表明，该分子由三个相同的α -1链组成。分枝重量来自基底膜的α -1链为108，000;它比间质胶原α -1链高出归因于过量己糖的量。化学分析显示高羟基赖氨酸，羟脯氨酸和甘氨酸含量和低量的丙氨酸。有8个半胱氨酸残基。总碳水化合物约为12%，由等摩尔量的葡萄糖和半乳糖组成。
Chromatographic studies on CM-cellulose of collagens isolated from basement membranes of the glomerulus, lens capsule and Descemet's membrane indicate that the molecule is composed of three identical α -1 chains. The M. Wt. of the α -1 chains from basement membranes is 108,000; it is higher than that of α -1 chains of interstitial collagens by an amount attributed to the excess hexose. Chemical analyses reveal high hydroxylysine, hydroxyproline and glycine content and a low amount of alanine. There are 8 residues of half-cystine. Total carbohydrate is about 12%, consisting of equimolar amounts of glucose and galactose.