Gopalakrishnan S, Boyle D, Takemoto L
Division of Biology, Kansas State University, Manhattan 66506-4901.
Invest Ophthalmol Vis Sci. 1994 Feb;35(2):382-7.
To characterize the possible interaction of alpha crystallin with partially denatured forms of gamma crystallin.
Gamma crystallin was denatured in the presence of guanidine hydrochloride, then dialyzed in the presence or absence of alpha crystallin. The high-molecular-weight complex formed in the presence of alpha was characterized by gel filtration chromatography, electron microscopy, and quantitative Western blot analysis.
Relative to native alpha or reconstituted aggregates of purified alpha, the higher molecular weight complex possessed a greater mean diameter and contained increased amounts of gamma crystallin.
Alpha crystallin preferentially interacts with partially denatured forms of a lens protein, consistent with its putative role as a functional molecular chaperone in the intact lens.
表征α-晶状体蛋白与部分变性形式的γ-晶状体蛋白之间可能的相互作用。
γ-晶状体蛋白在盐酸胍存在下变性，然后在有或没有α-晶状体蛋白存在的情况下进行透析。通过凝胶过滤色谱、电子显微镜和定量蛋白质免疫印迹分析对在α-晶状体蛋白存在下形成的高分子量复合物进行表征。
相对于天然α-晶状体蛋白或纯化α-晶状体蛋白的重构聚集体，更高分子量的复合物具有更大的平均直径，并且含有增加量的γ-晶状体蛋白。
α-晶状体蛋白优先与晶状体蛋白的部分变性形式相互作用，这与其在完整晶状体中作为功能性分子伴侣的假定作用一致。
