Fluorescence studies of human semi-beta-hemoglobin assembly

Biochemical and Biophysical Research Communications
F ChiuM J McDonald

Abstract

The intrinsic fluorescence properties of human alpha apohemoglobin at protein concentrations from 1 to 5 microM in 0.1 M potassium phosphate buffer, pH 7 or 8 at 5 degrees C were monitored in the absence and presence of a fixed concentration (5 microM) of a fluorescence quenching heme-containing native or Des (146-His, 145-Tyr) beta chain partner. These "reverse quenching" studies revealed that the emission intensity changes observed correlated well with protein concentration and theoretical extent of semi-beta-hemoglobin assembly. Furthermore, the relative quenching efficiencies were calculated to be 0.32, 0.25 and 0.61 for beta (pH 7), beta (pH 8) and Des beta (pH 7) chains, respectively. Thus, heme-mediated quenching was sensitive to the expected pH induced alpha apohemoglobin conformational change and to alteration in beta chain structure. Intramolecular changes induced by carboxylterminal modification (decreased "beta chain self-quenching") appeared to enhance the intermolecular rearrangements (increased "alpha chain partner quenching") seen upon subunit assembly.

References

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Citations

Sep 19, 2006·Journal of the American Society for Mass Spectrometry·Brian L Boys, Lars Konermann
Nov 12, 2013·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Jianbo LiuQinglin Sheng
Jul 17, 1999·Analytical Chemistry·C K LariveS Bogdanowich-Knipp

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