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一种天然胎盘基底膜胶原蛋白及其α链成分的分离与特性研究

Isolation and characterization of a native placental basement-membrane collagen and its component alpha chains.

作者信息

Glanville R W, Rauter A, Fietzek P P

出版信息

Eur J Biochem. 1979 Apr 2;95(2):383-9. doi: 10.1111/j.1432-1033.1979.tb12976.x.

Abstract

Native type IV collagen was isolated from human placenta using pepsin solubilisation followed by fractional salt precipitation and chromatogarphic purification. The native preparation was characterised using amino acid analyses, disc gel electrophoresis, segment-long-spacing crystallites and immunological methods. Two component alpha chains were isolated with molecular weights of approximately 95000 and 70000. Cyanogen bromide digests of these chains indicated that they are not related to any of the known alpha chains of interstitial collagens or to the recently described collagen containing alphaA and alphaB chains. They are also not related to one another and are therefore probably fragments of two genetically distinct type IV collagen alpha chains.

摘要

通过胃蛋白酶溶解,随后进行分级盐沉淀和色谱纯化,从人胎盘中分离出天然IV型胶原。使用氨基酸分析、圆盘凝胶电泳、片段长间距微晶和免疫学方法对天然制剂进行表征。分离出两条组分α链,分子量分别约为95000和70000。这些链的溴化氰消化表明,它们与间质胶原的任何已知α链或最近描述的含有αA和αB链的胶原均无关联。它们彼此之间也没有关系,因此可能是两条基因不同的IV型胶原α链的片段。

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