Fluorescence study of the conformational properties of myoglobin structure. 1. pH-dependent changes of tryptophanyl fluorescence in intact and chemically modified sperm whale apomyoglobins

The pH-dependent fluorescence of intact sperm whale apomyoglobin (apo-Mb) containing two tryptophans at positions 7 and 14, and of apo-Mb derivatives modified on Trp7 by 2-hydroxy-5-nitrobenzyl bromide (Koshland reagent) and o-nitrophenylsulphenyl chloride, has been studied. The fluorescence of apom...

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Veröffentlicht in:	European journal of biochemistry 1991-05, Vol.198 (1), p.223-232
Hauptverfasser:	Postnikova, G B, Komarov, Y E, Yumakova, E M
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoproteins - chemistry Fluorescence Polarization Hydrogen-Ion Concentration Myoglobin - chemistry Protein Conformation Spectrophotometry, Ultraviolet Tryptophan - chemistry Whales
Online-Zugang:	Volltext
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