Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin

Studies of the binding of N -methyl nicotinamide chloride by α-lactalbumin show that complex formation occurs with 1 of 4 tryptophan residues at pH 6 whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in exposure of tryptophans,...

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Veröffentlicht in:The Journal of biological chemistry 1972-05, Vol.247 (10), p.3062
Hauptverfasser: Frederick M. Robbins, Leo G. Holmes
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creator Frederick M. Robbins
Leo G. Holmes
description Studies of the binding of N -methyl nicotinamide chloride by α-lactalbumin show that complex formation occurs with 1 of 4 tryptophan residues at pH 6 whereas two form complexes at pH 2 as a result of acid denaturation. Alkaline denaturation likewise leads to an increase in exposure of tryptophans, and three of the four groups form complexes at pH 11. From a consideration of previous studies and a recently proposed molecular model for α-lactalbumin, the residues involved in binding N -methyl nicotinamide chloride have been tentatively identified as tryptophan-118, tryptophan-104, and tryptophan-60.
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title Binding of N-Methyl Nicotinamide Chloride by Tryptophan Residues of α-Lactalbumin
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