Stevens A, Walsh R, Augusteyn R C
National Vision Research Institute, Carlton, Victoria, Australia.
Curr Eye Res. 1996 Feb;15(2):215-8. doi: 10.3109/02713689608997416.
Complexes containing alpha-crystallin were isolated from crosslinked lens extract using an affinity column constructed with monoclonal antibodies specific for alpha-crystallin. The affinity-purified protein was compared with alpha-crystallins before and after crosslinking. Electron microscopy revealed sheet-like structures in the cross-linked protein from the lens extract compared with spherical structures for the others. Studies on the amino acid composition, tryptophan microenvironments and the interaction with a monoclonal antibody revealed that the complexes consist almost entirely of alpha-crystallin. These results indicate that under certain conditions, alpha-crystallin subunits can adopt a sheet-like form.
使用针对α-晶状体蛋白构建的亲和柱,从交联的晶状体提取物中分离出含有α-晶状体蛋白的复合物。将亲和纯化的蛋白质与交联前后的α-晶状体蛋白进行比较。电子显微镜显示,晶状体提取物中交联蛋白呈片状结构,而其他的则呈球形结构。对氨基酸组成、色氨酸微环境以及与单克隆抗体相互作用的研究表明,这些复合物几乎完全由α-晶状体蛋白组成。这些结果表明,在某些条件下,α-晶状体蛋白亚基可以呈现片状形式。