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Proteolysis of bovine F-actin by cathepsin D (E.C. 3.4.23.5) in 50 mM Na acetate buffer, pH 5.5, at 37 o C was investigated using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and reverse-phase high performance liquid chromatography (RP-HPLC). Actin was hydrolyzed by cathepsin D during incubation to peptides detectable by RP-HPLC, although no degradation products were...
The proteolytic specificity of cathepsin B on bovine F-actin was investigated. Actin (0.5 mg/ml) was incubated with cathepsin B (1.65 U/ml) for 6 h at 37 o C and samples were taken periodically for analysis by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). During incubation, actin was hydrolysed with the simultaneous appearance of three peptides detectable by SDS-PAGE...
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