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生物物理学报 1992
FORMATION OF POTASSIUM IODIDE FLUORESCENT DERIVATIVES OF CARBOXYMETHYLATION AND NAD DERIVATIVES OFYEAST D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
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Abstract:
Although tetrakiscarboxymethylated or biscarboxymethylated enzyme has not formed the fluorophore emitting 383 nm fluorescence with potassium iodide, each of them can emit the fluorescence after incubated with NAD+ for 30 h in the solution, but the control sample has little appreciable 383 nm emission by NAD+ dissolved with the potassium iodide. Nevertheless, NAD fluorescence derivative corresponding the tetrakiscarboxymethylated and biscarboxy-thylated enzyme can form the fluorophore of 383 nm with potassium iodide. Some differences in concentration of potassium iodide for optimum formation of 383 nm fluorophore between the tetrakiscarboxymethylated and the biscar-boxymethylated enzymes, as well as their corresponding NAD derivatives have been demonstrated. It appears that the fluorophore derivative may be near or at the active site, since formation of 383 nm fluorescence demands of GAPDH together with NAD + , which is appreciably effected by the amount of modific-cation of Cys-149.