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Proceedings Paper

Frequency domain lifetimes of liganded and unliganded hemoglobin measured with a 10-GHz instrument using front face geometry on a free liquid surface
Author(s): Enrico Bucci; Zygmunt Gryczynski; Clara Fronticelli; Gabor Laczko; Henryk M. Malak; Joseph R. Lakowicz
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Paper Abstract

We present data on lifetimes of hemoglobin solutions obtained using a 10 GHz frequency domain fluorometer and a specially designed cuvette which allows front face excitation on a free liquid surface. The cuvette eliminates reflections and stray emissions, which become significant for low intensity fluorophores like hemoglobin. Three lifetimes are detectable in the subnanosecond range. At high frequency it is possible to detect components below 10 ps. The average lifetime of hemoglobin is ligand dependent, opening a new chapter in the investigation of the allosteric behavior of hemoglobin.

Paper Details

Date Published: 1 May 1990
PDF: 7 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17742
Show Author Affiliations
Enrico Bucci, Univ. of Maryland at Baltimore (United States)
Zygmunt Gryczynski, Univ. of Maryland at Baltimore (United States)
Clara Fronticelli, Univ. of Maryland at Baltimore (United States)
Gabor Laczko, Univ. of Maryland at Baltimore (United States)
Henryk M. Malak, Univ. of Maryland at Baltimore (United States)
Joseph R. Lakowicz, Univ. of Maryland (United States)


Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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