The tryptophan fluorescence quenching by NADH or NAD in horse liver alcohol dehydro‐genase is investigated. Evidence is given that only one of the two tryptophan residues present in each subunit chain of the enzyme undergoes the quenching process. Such a quenching allows one to titrate exactly the enzyme active sites and to evaluate coenzyme binding constants. This quenching is then ascribed to a specific interaction between coenzyme and enzyme active site. The possible nature of this interaction is discussed.
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Luisi et al. (1970) studied this question.
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