Scott G, Mowrey-McKee M
Ciba Vision Corporation, Duluth, Georgia 30136 USA.
Curr Eye Res. 1996 May;15(5):461-6. doi: 10.3109/02713689609000757.
Following the solubilization of protein from patient worn soft contact lenses and subsequent analysis via SDS-PAGE, an unidentified 30 kDa protein deposit was commonly observed. The mysterious deposit was found to accumulate on a variety of soft contact lens material.
Acuvue, Cibasoft, Excelens and Newvue soft contact lenses were worn by three asymptomatic patients using both daily-wear and extended wear regimens. To characterize the unknown deposit, human tear samples and lens eluted protein were subjected to SDS-PAGE, immunoblotting, enzymatic assays and protein sequencing.
Results show that the 30 kDa protein deposit is the homologous dimer of tear lysozyme. Polymerized lysozyme was found on each of the three lens materials within one h of wear. However, the dimer was not present in the normal tear film.
Therefore, this dimerization phenomenon is the result of an aggregation and interaction of lysozyme with various soft contact lens polymers.
从患者佩戴过的软性隐形眼镜中提取蛋白质并通过SDS-PAGE进行后续分析后，通常会观察到一种未知的30 kDa蛋白质沉积物。发现这种神秘的沉积物会在多种软性隐形眼镜材料上积聚。
三名无症状患者使用日戴和长戴方案佩戴了酷柏、视康、爱维伦思和新悦软性隐形眼镜。为了表征这种未知沉积物，对人泪液样本和镜片洗脱蛋白进行了SDS-PAGE、免疫印迹、酶活性测定和蛋白质测序。
结果表明，30 kDa蛋白质沉积物是泪液溶菌酶的同源二聚体。佩戴一小时内，在三种镜片材料上均发现了聚合溶菌酶。然而，正常泪膜中不存在这种二聚体。
因此，这种二聚化现象是溶菌酶与各种软性隐形眼镜聚合物聚集和相互作用的结果。
