人类胎盘胶原蛋白的A链和B链在单个三螺旋中组装的物理证据。

Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helix.

作者信息

Bentz H, Bächinger H P, Glanville R, Kühn K

出版信息

Eur J Biochem. 1978 Dec;92(2):563-7. doi: 10.1111/j.1432-1033.1978.tb12778.x.

DOI:10.1111/j.1432-1033.1978.tb12778.x

Abstract

Native collagen molecules containing A and B chains were isolated from pepsin-solubilised human chorionic and amniotic membrane extracts by fractional salt precipitation and DEAE-cellulose chromatography. They exhibited a circular dichroism spectrum, and a melting curve, characteristic for a triple-helical structure. Electron microscopical investigations of their segment-long-spacing crystallites revealed a molecule similar to those of the interstitial types I, II and III collagens. After denaturation, the A and B chains were separated by DEAE-cellulose chromatography and were consistently recovered in a ratio of 1:2. Renaturation experiments indicated that only the B chains are able to reform triple-helical molecules which are stable under conditions in vivo. The data support a molecular formula A(B)2 for the native collagen molecule.

摘要

通过分级盐沉淀和DEAE-纤维素色谱法，从胃蛋白酶溶解的人绒毛膜和羊膜提取物中分离出含有A链和B链的天然胶原蛋白分子。它们呈现出圆二色光谱和熔解曲线，这是三螺旋结构的特征。对其片段长间距微晶的电子显微镜研究表明，该分子与I型、II型和III型间质胶原分子相似。变性后，通过DEAE-纤维素色谱法分离出A链和B链，且始终以1:2的比例回收。复性实验表明，只有B链能够重新形成在体内条件下稳定的三螺旋分子。这些数据支持天然胶原蛋白分子的分子式为A(B)2。