胶原蛋白交联的化学性质。从含有未知氨基酸的成熟胶原蛋白中纯化和鉴定交联聚合肽材料。
The chemistry of the collagen cross-links. Purification and characterization of cross-linked polymeric peptide material from mature collagen containing unknown amino acids.
作者信息
Light N D, Bailey A J
出版信息
Biochem J. 1980 Feb 1;185(2):373-81. doi: 10.1042/bj1850373.
Abstract
A polymeric form of the alpha 1-chain C-terminal peptide alpha 1 CB6 (poly-alpha 1 CB6) was purified from CNBr digests of insoluble bovine tendon type-I-collagen by gel filtration and ion-exchage chromatography. The purified material had a molecular weight of 1.5 x 10(6)-5 x 10(6) on gel filtration and an amino acid content virtually identical with that of monomeric peptide alpha 1 CB6. The material could be adsorbed on affinity gels containing immobilized anti-(alpha 1 CB6-peptide non-helical region) antibodies and was an inhibitor of haemagglutination by the same antibodies of alpha 1 CB6-peptide-coated sheep erythrocytes. Periodate treatment of the material had no effect. Alkali hydrolysates were shown to contain two unknown amino acids, which were purified by gel filtration and ion-exchange chromatography in volatile buffers and are believed to be components of the mature cross-link of collagen.
摘要
从不溶性牛肌腱I型胶原蛋白的溴化氰消化产物中，通过凝胶过滤和离子交换色谱法纯化出α1链C末端肽α1 CB6的聚合形式（聚-α1 CB6）。纯化后的物质在凝胶过滤中的分子量为1.5×10⁶ - 5×10⁶，其氨基酸含量与单体肽α1 CB6几乎相同。该物质可吸附在含有固定化抗（α1 CB6肽非螺旋区）抗体的亲和凝胶上，并且是α1 CB6肽包被的绵羊红细胞被相同抗体进行血凝反应的抑制剂。高碘酸盐处理该物质没有效果。碱水解产物显示含有两种未知氨基酸，通过在挥发性缓冲液中的凝胶过滤和离子交换色谱法对其进行纯化，据信它们是胶原蛋白成熟交联的成分。
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本文引用的文献
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