Fluorescence has not been previously detected in intact hemoproteins. We have been able to measure significant fluorescence emission in purified oxy HbA using front-face fluorometry. The excitation maximum (293 nm), the emission maximum (325 nm) and the fluorescence spectra of Hb Rothschild (β 37 Trp → Arg) allows us to conclude that β 37 Trp is primarily responsible for the fluorescence signal of HbA. We propose that this intrinsic fluorescence of hemoglobin may be used as a probe to study conformational changes in hemoglobin and possibly other heme-containing proteins.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Mar 28 1980|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology