1.
Biophys Chem
; 30(2): 105-12, 1988 Jun.
Artigo
em Inglês
| MEDLINE
| ID: mdl-3416039
RESUMO
Decay curves for tryptophan fluorescence of bovine and human alpha-lactalbumin in different states (metal-free and Ca2+ or Mg2+-loaded states of the native and thermally denatured proteins) have been measured at different wavelengths. The curves are best fitted by a sum of three exponents assigned to emission of individual tryptophan residues. The results suggests that the red shift of the fluorescence spectrum of alpha-lactalbumin caused by release of the bound Ca2+ or thermal denaturation is due to changes in the environment of all emitting tryptophan residues.