PURPOSE: 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. METHODS: 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: 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. CONCLUSIONS: Therefore, this dimerization phenomenon is the result of an aggregation and interaction of lysozyme with various soft contact lens polymers.
PURPOSE: 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. METHODS: 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: 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. CONCLUSIONS: Therefore, this dimerization phenomenon is the result of an aggregation and interaction of lysozyme with various soft contact lens polymers.