Time-resolved fluorescence of hemoglobin species

Zygmunt Gryczynski, Sabrina Beretta, Jacek Lubkowski, Anna Razynska, Ignacy Gryczynski, Enrico Bucci

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

We used time-resolved fluorescence in the pico- to nanosecond time range to monitor the presence of tetramers, dimers and monomers in carbonmonoxyhemoglobin (COHb) solutions and to investigate how their distributions change under different experimental conditions. Comparison of fluorescence lifetime computed from the atomic coordinates of COHb (Vasquez et al., 1996) with those experimentally measured allowed identification of molecular species present in the hemoglobin solution. It was possible to observe modification of the distribution of tetramers, dimers, monomers and species with disordered hemes produced by different experimental conditions. Protein concentration affected the detectable lifetimes, indicating increasing amounts of dimers and monomers at low protein concentrations, while the amount of inverted hemes was not modified. Titration with up to 1 M NaCl modified only the extent of dissociation of hemoglobin into dimers, without affecting heme inversion and monomer formation. Hyperbaric pressure increased the amounts of dimers and monomers. This is the first time that monomeric subunits of hemoglobin have been detected at neutral pH in the normal system.

Original languageEnglish
Pages (from-to)81-91
Number of pages11
JournalBiophysical Chemistry
Volume64
Issue number1-3
DOIs
StatePublished - 28 Feb 1997

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Heme
Dimers
Carboxyhemoglobin
Hemoglobins
Monomers
Fluorescence
Hemoglobin Subunits
Proteins
Pressure
Titration

Keywords

  • Fluorescence lifetime
  • Hemoglobin species
  • Time-resolved fluorescence

Cite this

Gryczynski, Zygmunt ; Beretta, Sabrina ; Lubkowski, Jacek ; Razynska, Anna ; Gryczynski, Ignacy ; Bucci, Enrico. / Time-resolved fluorescence of hemoglobin species. In: Biophysical Chemistry. 1997 ; Vol. 64, No. 1-3. pp. 81-91.
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Time-resolved fluorescence of hemoglobin species. / Gryczynski, Zygmunt; Beretta, Sabrina; Lubkowski, Jacek; Razynska, Anna; Gryczynski, Ignacy; Bucci, Enrico.

In: Biophysical Chemistry, Vol. 64, No. 1-3, 28.02.1997, p. 81-91.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Gryczynski, Zygmunt

AU - Beretta, Sabrina

AU - Lubkowski, Jacek

AU - Razynska, Anna

AU - Gryczynski, Ignacy

AU - Bucci, Enrico

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