The intrinsic fluorescence of the recombinant human leukocyte interferon-alpha A and fibroblast interferon-beta 1.
The environment of Trp residues of the recombinant human interferons has been studied by the analysis of the emission spectra of native and denatured proteins at pH 1.5-8.5 and temperature 10-65 degrees C in the presence and absence of the anionic, cationic and neutral to charge contact quenchers--KI, CsCl and acrylamide, respectively. The obtained data allow to suppose that in IFN-alpha A and IFN-beta 1 Trp141 interacts with Arg145 and one or several from the following residues--Phe124, Ile127, Tyr130, Leu131, whereas Trp77--with Arg33 and Phe36, Phe78, Leu81 or Leu82 (Ile81 or Val82 for IFN-beta 1).
Borukhov
S I
SI
Institute of Molecular Genetics, USSR Academy of Sciences, Moscow.
Strongin AYa
D005453:Fluorescence; D006801:Humans; D007370:Interferon Type I / Q000032:analysis*; D000077190:Interferon alpha-2; D016898:Interferon-alpha / Q000032:analysis*; D011487:Protein Conformation; D011994:Recombinant Proteins; D014364:Tryptophan / Q000032:analysis*
D007370:Interferon Type I; D000077190:Interferon alpha-2; D016898:Interferon-alpha; D011994:Recombinant Proteins; D014364:Tryptophan