Abstract
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) |
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Pages (from-to) | 432-439 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 93 |
Issue number | 2 |
DOIs | |
State | Published - Mar 28 1980 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology