Characterization of human serum albumin forms with pH. Fluorescence lifetime studies.
Fluorescence lifetimes of human serum albumin (HSA) tryptophan 214 residue were measured in solution at different pH (from 2 to 12). The results indicate that tryptophan emission occurs with three lifetimes at all pH. However, lifetimes and pre-exponential values are dependent on the pH and thus on the protein form. Three different protein populations have been differentiated: one population for pH 2 and 3 (extended form), the second one from pH 4 to 9 containing HSA migrating (F), normal (N) and basic (B) forms. Another type of population is obvious for pH higher than 9, characterizing the aged (A) form of HSA.
Amiri
Megdouda
M
Laboratoire de Biophysique Moléculaire, Université des Sciences et Technologies de Lille, Bâtiment C6, 59655 Villeneuve d'Ascq Cédex, France.
Jankeje
Kristina
K
Albani
Jihad René
JR
D005453:Fluorescence; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D020033:Protein Isoforms; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014364:Tryptophan
D020033:Protein Isoforms; D012709:Serum Albumin; D014364:Tryptophan