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从各种人体组织中制备的聚合胶原蛋白的分离及其氨基酸和碳水化合物组成。

The isolation, and amino acid and carbohydrate composition, of polymeric collagens prepared from various human tissues.

作者信息

Schofield J D, Freeman I L, Jackson D S

出版信息

Biochem J. 1971 Sep;124(3):467-73. doi: 10.1042/bj1240467.

Abstract
  1. Insoluble polymeric collagens from various human tissues were prepared by the EDTA method. Almost all of the collagen from simple soft tissues such as dermis, tendon, submucosa, sclera and cornea could be extracted, whereas the more complex tissues such as intercostal cartilage and intervertebral disc yielded only small amounts of collagen. Amino acid and carbohydrate analysis indicated that most of the preparations were highly purified on the basis of their tyrosine, hexosamine, mannose, xylose and fucose contents. 2. Wide variation in the total hexose content was observed, the lowest being 8.5 residues/3000 amino acid residues for collagen from dermis and the highest being 42.1 residues/3000 in corneal collagen. The molar ratios of sugars also varied, submucosal collagen having a galactose/glucose ratio of 1.0 and corneal collagen having a ratio of 2.3. 3. The presence of glucosylgalactosylhydroxylysine was confirmed in submucosal collagen by compositional and chromatographic analysis of this component after its isolation from alkaline hydrolysates of the collagen. Evidence was also obtained for the presence of galactosylhydroxylysine. 4. Determination of the hydroxylysyl glycosides was carried out and it was observed that the amounts of these components varied widely from tissue to tissue. Corneal collagen contained 19.1 hydroxylysine-linked carbohydrate units/3000 amino acid residues, whereas tendon collagen contained only 4.1 units/3000. Variation in the ratio disaccharide unit/monosaccharide unit was also observed, the ratio being 1.2 in intercostal cartilage collagen and 4.1 in submucosal collagen. The proportion of the total hydroxylysine that was substituted by carbohydrate also varied from tissue to tissue.
摘要
  1. 采用乙二胺四乙酸(EDTA)法制备了来自各种人体组织的不溶性聚合胶原蛋白。几乎所有来自真皮、肌腱、黏膜下层、巩膜和角膜等简单软组织的胶原蛋白都能被提取出来,而肋软骨和椎间盘等更复杂的组织仅能提取出少量胶原蛋白。氨基酸和碳水化合物分析表明,大多数制剂基于其酪氨酸、己糖胺、甘露糖、木糖和岩藻糖含量而言已高度纯化。2. 观察到总己糖含量存在广泛差异,真皮胶原蛋白中最低为8.5个残基/3000个氨基酸残基,角膜胶原蛋白中最高为42.1个残基/3000个。糖的摩尔比也有所不同,黏膜下层胶原蛋白的半乳糖/葡萄糖比为1.0,角膜胶原蛋白的该比例为2.3。3. 通过从胶原蛋白碱性水解物中分离出该成分后对其进行组成和色谱分析,证实黏膜下层胶原蛋白中存在葡萄糖基半乳糖基羟赖氨酸。还获得了半乳糖基羟赖氨酸存在的证据。4. 对羟赖氨酸糖苷进行了测定,观察到这些成分的含量因组织而异。角膜胶原蛋白含有19.1个羟赖氨酸连接的碳水化合物单位/3000个氨基酸残基,而肌腱胶原蛋白仅含有4.1个单位/3000。二糖单位/单糖单位的比例也存在差异,肋软骨胶原蛋白中的比例为1.2,黏膜下层胶原蛋白中的比例为4.1。被碳水化合物取代的总羟赖氨酸比例也因组织而异。

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