1,8-Anilinonaphthalene sulfonate binds to central cavity of human hemoglobin

Binding of 1,8-anilinonaphthalene sulfonate (1,8-ANS) to main (HbA 1) and glycosylated (HbA 1C) forms of human oxyhemoglobin in the presence/absence of inositolhexaphosphate (IHP) in 50 mM potassium phosphate buffer, pH 7.4, was studied by time-correlated single photon counter with subnanosecond tim...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2004-05, Vol.317 (3), p.761-767
Main Authors: Syakhovich, Vitaly E., Parul, Dmitry A., Ruta, Ekaterina Ya, Bushuk, Boris A., Bokut, Sergey B.
Format: Article
Language:English
Subjects:
1,8-Anilinonaphthalene sulfonate
Adult
Anilino Naphthalenesulfonates - metabolism
DPG-binding site
Glycosylated hemoglobin
Hemoglobins - metabolism
Humans
Inositolhexaphosphate
Oxyhemoglobin
Protein Binding
Time-resolved spectrofluorimetry
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Summary:Binding of 1,8-anilinonaphthalene sulfonate (1,8-ANS) to main (HbA 1) and glycosylated (HbA 1C) forms of human oxyhemoglobin in the presence/absence of inositolhexaphosphate (IHP) in 50 mM potassium phosphate buffer, pH 7.4, was studied by time-correlated single photon counter with subnanosecond time resolution. The redistribution of contributions of the most long-lived and the most short-lived fluorescent decay components in the presence of IHP provides an evidence of the probe binding within oxyhemoglobin central cavity, namely DPG-binding site. Finally, it was shown that the fluorescent probe is extremely sensitive for hemoglobin central cavity modification, provided by the carbohydrate moiety in case of 1,8-ANS interactions with HbA 1C.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.03.111