Biochemical and Biophysical Research Communications
Tryptophan fluorescence of human hemoglobin. I. Significant change of fluorescence intensity and lifetimes in the T − R transition☆
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Characteristic emission in glutaraldehyde polymerized hemoglobin
2011, Journal of LuminescenceCitation Excerpt :The excitation and emission maxima were observed at around 280 and 320 nm, respectively. The dynamical processes of tryptophan emission were studied at low hemoglobin concentration in 1981 [14]. Longer wavelength emissions from heme degradation compounds I and II were studied later on and interpreted as ferryl (Fe4+) heme degradation associated fluorescence during the reaction of Hb with hydrogen peroxide (H2O2) and in the process of auto-oxidation [15,16].
A fluorimetric and circular dichroism study of hemoglobin - Effect of pH and anionic amphiphiles
2006, Journal of Colloid and Interface ScienceCitation Excerpt :For example, transport from the lungs (pH 7.4) to active muscle (pH 7.2) results in an oxygen release amounting to 77% of the total oxygen-carrying capacity (whereas normally 66% of oxygen would be released). Change in oxygen-binding capacity leads to a change in quaternary structure of Hb from the R (oxy form) to the T (deoxy form), as mentioned in Section 1, [1–6,16,17]. We assign the form of Hb existing at pH < 3 to the well-known T form and the form existing above this pH to the R form.
Distinct domain responses of R-state human hemoglobins A, C, and S to anions
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1997, Comparative Biochemistry and Physiology - A PhysiologyConformational changes in oxyhemoglobin C (Glu<sup>β6</sup> → Lys) detected by spectroscopic probing
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1995, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
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A preliminary report was presented in the Japanese Symposium of Photochemistry (Abstract p. 142), Tokyo, December 1979.