胃蛋白酶溶解的人肾小球基底膜胶原蛋白的异质性

Heterogeneity of pepsin-solubilized human glomerular basement membrane collagen.

作者信息

Tryggvason K, Kivirikko K I

出版信息

Nephron. 1978;21(4):230-5. doi: 10.1159/000181397.

Abstract

The collagen component of isolated glomerular basement membrane ws solubilized by limited pepsin digestion and further purified. The amino acid and carbohydrate composition of the final material was very similar to that described for the alpha1-chains of type IV collagen. However, the presence of several components was detected when the material was analyzed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis either without or after reduction. The molecular weights of the major components in the reduced material were about 140,000, 100,000, 80,000 and less than 65,000 (in the case of five components). The data thus do not support the previous suggestion that the human glomerular basement membrane contains only one type of collagen polypeptide chain. However, part of the heterogeneity may be due to the presence of more than one collagenous part in a procollagen-type polypeptide chain, and an additional reason may lie in a partial degradation of collagenous portions during pepsin digestion.

摘要

分离出的肾小球基底膜的胶原蛋白成分经有限的胃蛋白酶消化后可溶解并进一步纯化。最终产物的氨基酸和碳水化合物组成与IV型胶原蛋白α1链的描述非常相似。然而，当该物质在还原或未还原的情况下通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行分析时，检测到了几种成分。还原物质中主要成分的分子量约为140,000、100,000、80,000以及小于65,000（对于五种成分而言）。因此，这些数据不支持先前关于人肾小球基底膜仅包含一种胶原蛋白多肽链的观点。然而，部分异质性可能是由于前胶原型多肽链中存在不止一个胶原部分，另一个原因可能在于胃蛋白酶消化过程中胶原部分的部分降解。