Distribution of fluorescence decay times for 1-anilinonaphthalene-8-sulfonate in human oxyhemoglobin A1b solution

We have studied complex formation between molecules of the fluorescent probe 1-anilinonaphthalene-8-sulfonate (1,8-ANS) and the major form (A 1 ) and a minor form (A b ) of hemoglobin. The contribution of the longlived component f 3 to the kinetic curves for fluorescence decay in HbA 1b solutions is...

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Bibliographic Details
Published in:Journal of applied spectroscopy 2012-07, Vol.79 (3), p.437-445
Main Authors: Drazdou, A. S., Sobchuk, A. N., Syakhovich, V. E., Bokut, O. S., Kvasyuk, E. I., Bushuk, B. A., Bokut, S. B.
Format: Article
Language:English
Subjects:
Analytical Chemistry
Atomic/Molecular Structure and Spectra
Physics
Physics and Astronomy
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Summary:We have studied complex formation between molecules of the fluorescent probe 1-anilinonaphthalene-8-sulfonate (1,8-ANS) and the major form (A 1 ) and a minor form (A b ) of hemoglobin. The contribution of the longlived component f 3 to the kinetic curves for fluorescence decay in HbA 1b solutions is 0.021–0.036, which indicates a dramatic decrease (compared with HbA 1 ) in the accessibility of the central cavity of HbA 1b for binding 1,8-ANS. Disappearance of the long-lived component f 3 in the fluorescence decay kinetics of 1,8-ANS in HbA 1b solutions in the presence of inositol hexaphosphate (IHP) suggests that the regulatory region of HbA1b is completely inaccessible for interaction both with the negatively charged molecules of the probe and with natural regulators of the transport function for this form of the heme protein.
ISSN:0021-9037
1573-8647
DOI:10.1007/s10812-012-9620-4