来自小牛晶状体核的高分子量α-晶状体蛋白亚群的物理化学特性

Physicochemical characterization of high-molecular-weight alpha-crystallin subpopulations from the calf lens nucleus.

作者信息

Siezen R J, Owen E A

出版信息

Biochim Biophys Acta. 1983 Dec 28;749(3):227-37. doi: 10.1016/0167-4838(83)90229-7.

Abstract

Calf lens nuclear alpha-crystallin was separated into five molecular weight subpopulations by exclusion chromatography on Bio-Gel A-5m. These subpopulations were compared by amino acid analysis, ultraviolet absorption analysis, fluorescence, far- and near-ultraviolet circular dichroism, isoelectric focusing, SDS-polyacrylamide gel electrophoresis and sedimentation velocity analysis. Although only minor differences were detectable in most physicochemical properties, progressive changes were found in the near-ultraviolet circular dichroism spectra and in pellet hardness after centrifugation. Minute amounts of beta-crystallin polypeptides and a 43 kDa component were present in all five subpopulations. In addition, the highest molecular weight aggregates contain some gamma-crystallin polypeptides. A slow re-equilibration of separated subpopulations towards the initial distribution was observed by rechromatography.

摘要

通过在Bio-Gel A-5m上进行排阻色谱法，将小牛晶状体核α-晶状体蛋白分离成五个分子量亚群。通过氨基酸分析、紫外吸收分析、荧光、远紫外和近紫外圆二色性、等电聚焦、SDS-聚丙烯酰胺凝胶电泳和沉降速度分析对这些亚群进行了比较。尽管在大多数物理化学性质中仅检测到微小差异，但在近紫外圆二色性光谱和离心后的沉淀硬度方面发现了渐进变化。所有五个亚群中均存在微量的β-晶状体蛋白多肽和一种43 kDa的成分。此外，分子量最高的聚集体包含一些γ-晶状体蛋白多肽。通过再色谱法观察到分离的亚群向初始分布的缓慢重新平衡。