Journal: Biochemical Journal

Article Title: Modification of luciferase to be a substrate for plant aspartic proteinase

doi: 10.1042/bj3430425

Figure Lengend Snippet: Figure 1 Loss of luciferase activity when incubated with the aspartic proteinase

Article Snippet: The supernatants were combined and dialysed against a luciferase storage buffer [1 mMEDTA}1 mMdithiothreitol (DTT)}25 mM Tris}acetate}0.2 M (NH % ) # SO % (pH 7.8)] with the use of a Sli- dalyzer dialysis cassette (Pierce, Rockford, IL, U.S.A.) at 25 °C for 4 h. The quantitative luminescence assay of the luciferase involved adding 5 μl of each sample (translated protein) to a well on a Packard Instrument Company (Meriden, CT, U.S.A.) HTRF black 96-well Optiplate containing 20 μl of a luciferase stabilization solution (1.25 mM MgCl # }1.25 mM CaCl # ).

Techniques: Luciferase, Activity Assay, Incubation

Journal: Biochemical Journal

Article Title: Modification of luciferase to be a substrate for plant aspartic proteinase

doi: 10.1042/bj3430425

Figure Lengend Snippet: Figure 2 Western blots of luciferase proteins during incubation with the aspartic proteinase

Article Snippet: The supernatants were combined and dialysed against a luciferase storage buffer [1 mMEDTA}1 mMdithiothreitol (DTT)}25 mM Tris}acetate}0.2 M (NH % ) # SO % (pH 7.8)] with the use of a Sli- dalyzer dialysis cassette (Pierce, Rockford, IL, U.S.A.) at 25 °C for 4 h. The quantitative luminescence assay of the luciferase involved adding 5 μl of each sample (translated protein) to a well on a Packard Instrument Company (Meriden, CT, U.S.A.) HTRF black 96-well Optiplate containing 20 μl of a luciferase stabilization solution (1.25 mM MgCl # }1.25 mM CaCl # ).

Techniques: Western Blot, Luciferase, Incubation

Journal: Biochemical Journal

Article Title: Modification of luciferase to be a substrate for plant aspartic proteinase

doi: 10.1042/bj3430425

Figure Lengend Snippet: Figure 3 Western blots of pSP-luc luciferase protein during incubation with clostripain

Article Snippet: The supernatants were combined and dialysed against a luciferase storage buffer [1 mMEDTA}1 mMdithiothreitol (DTT)}25 mM Tris}acetate}0.2 M (NH % ) # SO % (pH 7.8)] with the use of a Sli- dalyzer dialysis cassette (Pierce, Rockford, IL, U.S.A.) at 25 °C for 4 h. The quantitative luminescence assay of the luciferase involved adding 5 μl of each sample (translated protein) to a well on a Packard Instrument Company (Meriden, CT, U.S.A.) HTRF black 96-well Optiplate containing 20 μl of a luciferase stabilization solution (1.25 mM MgCl # }1.25 mM CaCl # ).

Techniques: Western Blot, Luciferase, Incubation

Journal: Biochemical Journal

Article Title: Modification of luciferase to be a substrate for plant aspartic proteinase

doi: 10.1042/bj3430425

Figure Lengend Snippet: Figure 4 Western blots of other luciferase proteins during incubation with the aspartic proteinase

Article Snippet: The supernatants were combined and dialysed against a luciferase storage buffer [1 mMEDTA}1 mMdithiothreitol (DTT)}25 mM Tris}acetate}0.2 M (NH % ) # SO % (pH 7.8)] with the use of a Sli- dalyzer dialysis cassette (Pierce, Rockford, IL, U.S.A.) at 25 °C for 4 h. The quantitative luminescence assay of the luciferase involved adding 5 μl of each sample (translated protein) to a well on a Packard Instrument Company (Meriden, CT, U.S.A.) HTRF black 96-well Optiplate containing 20 μl of a luciferase stabilization solution (1.25 mM MgCl # }1.25 mM CaCl # ).

Techniques: Western Blot, Luciferase, Incubation