[Anion-binding centers of human serum albumin during an N-F conformation transition and in isolated albumin and blood serum].
Fluorescent probe N-phenyl-1-amino-8-sulfonaphthalene (ANS) was used for studying pH-dependent structural N-F-transition in human serum albumin of two kinds: in commercial albumin and in natural blood serum. The kinetics of ANS fluorescence decay in albumin solutions was measured. There were found two types of the sites occupied by ANS in albumin under physiological conditions (pH 7.4). In the first binding site ANS fluorescence decay time was 16.6 +/- 0.3 nsec and it was not significantly changed at N-F transition (pH 4.0). In the second binding site the decay time was dependent on pH in commercial albumin and was not significantly changed in serum. In the second binding site there were individual differences of ANS decay time (4.3 +/- 0.6 nsec). The observed ANS fluorescence intensity enhancing (about 40-50%) in N-F transition may be explained by an increase of albumin binding sites capacity for ANS.
Miller
Iu I
IuI
Dobretsov
G E
GE
Kolchin
Iu A
IuA
D000817:Anilino Naphthalenesulfonates / Q000737:chemistry*; D000838:Anions; D001665:Binding Sites; D005456:Fluorescent Dyes; D006801:Humans; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism*
D000817:Anilino Naphthalenesulfonates; D000838:Anions; D005456:Fluorescent Dyes; D012709:Serum Albumin; C027132:1-anilino-8-naphthalenesulfonate
Anion-sviazyvaiushchie tsentry syvorotochnogo al'bumina cheloveka pri konformatsionnom perekhod N---F v vydelennom al'bumine i v syvorotke krovi.