Abstract
An increased ethidium bromide fluorescence at 610 nm was observed in the presence of cholinesterases from some natural sources, and a new fluorescence band appeared in the 500-570 nm region. The data obtained suggest a resonance energy transfer from the cholinesterase-ethidium bromide complex to a free ethidium bromide molecule. The structure of the peripheral ligand binding sites in the active center of bovine erythrocyte acetylcholinesterase, horse serum butyrylcholinesterase, and squid ganglia cholinesterase proved essentially similar.
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