Sack R A, Jones B, Antignani A, Libow R, Harvey H
Invest Ophthalmol Vis Sci. 1987 May;28(5):842-9.
The in-situ lens-bound protein layer (LBPL) was characterized on hydrogels of varying water content and ionic-binding capacity. The LBPL proved to be critically dependent on the ionic binding capacity of a given hydrogel. On nonionic polymers the LBPL invariably was thin and largely insoluble. Histochemical staining allowed the detection of all major types of tear proteins. Amino acid analysis revealed a variable composition. Extractable protein proved devoid of active lysozyme. Electrophoresis of pooled samples revealed a variable mixture of acidic, neutral, and basic bands. To what extent variability is dependent on tear film composition and lens structure awaits use of more sensitive analytic procedures. On anionic hydroxyethylmethacrylate copolymer lenses, the LBPL proved radically different. Here the LBPL invariably was much thicker and composed primarily of loosely bound protein. Electrophoresis and enzymatic analysis revealed a homogenous layer consisting primarily of lysozyme much of which retains enzymatic activity. The amino acid analysis of the insoluble protein suggests a similar composition. Specificity of deposition can be attributed to ionic affinity. Conformational integrity can be attributed partly to the unique stability of lysozyme. Electrophoresis of a pooled anionic lens extract revealed an unknown, highly mobile, basic protein. This presumably represents the selective accumulation of a highly basic trace or transient constituent of the tear film. The specificity and biological activity of the LBPL on the anionic lens may modify hydrogel biocompatibility affecting risk of spoilage, microbial colonization, and propensity to trigger an inflammatory and immune response.
对具有不同含水量和离子结合能力的水凝胶上的原位晶状体结合蛋白层（LBPL）进行了表征。结果证明，LBPL严重依赖于特定水凝胶的离子结合能力。在非离子聚合物上，LBPL总是很薄且基本上不溶。组织化学染色可检测到所有主要类型的泪液蛋白。氨基酸分析显示其组成可变。可提取的蛋白质被证明不含活性溶菌酶。合并样本的电泳显示出酸性、中性和碱性条带的可变混合物。变异性在多大程度上取决于泪膜组成和晶状体结构，尚有待使用更灵敏的分析程序来确定。在阴离子甲基丙烯酸羟乙酯共聚物晶状体上，LBPL被证明有根本不同。在这里，LBPL总是厚得多，主要由松散结合的蛋白质组成。电泳和酶分析显示有一层主要由溶菌酶组成的均匀层，其中许多溶菌酶保留了酶活性。不溶性蛋白质的氨基酸分析表明其组成相似。沉积的特异性可归因于离子亲和力。构象完整性可部分归因于溶菌酶独特的稳定性。合并的阴离子晶状体提取物的电泳显示出一种未知的、高度可移动的碱性蛋白质。这大概代表了泪膜中一种高度碱性的微量或短暂成分的选择性积累。阴离子晶状体上LBPL的特异性和生物活性可能会改变水凝胶的生物相容性，影响变质风险、微生物定植以及引发炎症和免疫反应的倾向。
