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 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | 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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ISSN: | 0021-9258 1083-351X |