Characterization and quantification of acid phosphatase and glycoside hydrolases in rabbit cornea.

The optimal reaction condition and kinetic properties of 8 lysosomal hydrolases in rabbit cornea determined with the use of fluorogenic derivatives of 4-methylumbelliferone are described. The enzymes studied were alpha- and beta-glucosidase alpha- and beta-galactosidase, alpha-mannosidase, beta-acetylglucosaminidase, beta-glucuronidase and acid phosphatase. Sodium taurocholate was an essential requirement for beta-glucosidase activity. Approximately the same pH optimum values, Michaelis-Menten constants and sensitivity to inhibitors were found as by other investigators in other tissues. The reaction conditions described in this report can be used for studying the influence of physical chemical, viral, bacterial agents etc. on the cornea and further also for the diagnosis of eventual lysosomal storage diseases.