Sredy J, Roy D, Spector A
Curr Eye Res. 1984 Dec;3(12):1423-31. doi: 10.3109/02713688409000838.
Two of the major in vitro phosphorylated polypeptides of the bovine lens have been identified. Analysis by means of two-dimensional gel electrophoresis (IEF) has demonstrated that the lens phosphorylated 57,000 and 43,000 dalton polypeptides correspond in mobility to purified phosphorylated bovine lens vimentin and chicken gizzard actin, respectively. Purified actin and vimentin were phosphorylated by a partially purified cAMP-dependent protein kinase isolated from the outer cortex water soluble fraction. All detectable bovine lens vimentin isoelectric variants were phosphorylated. In both the lens fiber cell and chicken gizzard actin preparations, the phosphorylated actin isoelectric variants did not correspond in mobility to the major actin isoelectric variant, but were more acidic. Phosphorylation in all preparations occurred at serine residues.
已鉴定出牛晶状体的两种主要体外磷酸化多肽。通过二维凝胶电泳（IEF）分析表明，晶状体磷酸化的57,000道尔顿和43,000道尔顿多肽的迁移率分别与纯化的磷酸化牛晶状体波形蛋白和鸡砂囊肌动蛋白相对应。从外皮质水溶性部分分离出的部分纯化的cAMP依赖性蛋白激酶将纯化的肌动蛋白和波形蛋白磷酸化。所有可检测到的牛晶状体波形蛋白等电变体均被磷酸化。在晶状体纤维细胞和鸡砂囊肌动蛋白制剂中，磷酸化的肌动蛋白等电变体的迁移率与主要的肌动蛋白等电变体不对应，而是更偏酸性。所有制剂中的磷酸化均发生在丝氨酸残基上。
