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- W2045443637 abstract "Abstract The protein fluorescence quenching of horse liver alcohol dehydrogenase (LADH) by p-chloromercuriphenyl sulfonate (PMS) was studied in the presence and absence of various enzyme ligands. The protein fluorescence was quenched by PMS upon formation of the mercaptides with sulfhydryl groups in LADH. The quenching of bound NADH fluorescence of the LADH-NADH and LADH-NADH-iso-butyramide complexes by PMS was studied comparatively and found to afford a method for investigating the mechanism of protein fluorescence quenching. The quenching mechanism appears to involve excitation energy transfer and denaturation of the enzyme. In addition, the release of ligand may also be involved in the mechanism. The formation of six enzyme-active modified forms of LADH by treatment of the enzyme with PMS was demonstrated by the fluorescence, activity, and electrophoretic measurements." @default.
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- W2045443637 date "1975-01-01" @default.
- W2045443637 modified "2023-10-14" @default.
- W2045443637 title "Fluorescence quenching of horse liver alcohol dehydrogenase and its complexes by para-chloromercuriphenyl sulfonate" @default.
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- W2045443637 doi "https://doi.org/10.1016/0003-9861(75)90358-6" @default.
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