Effects of wavelength on fitting Adair constants for binding of oxygen to human hemoglobin

Lawrence J Parkhurst, T. M. Larsen, H. Y. Lee

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

This chapter focuses on the effects of wavelength on fitting Adair constants for binding of oxygen (O2) to human hemoglobin (Hb). This chapter presents enzymatic depletion of O2 in the solution as an alternative to equilibration with a gas phase and the use of myoglobin as an O2 sensor to eliminate stirring altogether. However, a more recent study in the same wavelength region concluded that the apparent binding constants were indeed wavelength dependent. In using an oxygen electrode, a procedure to smooth the data using exponential splines has been developed that is appropriate when the deoxygenation process, as carried out enzymatically, can be regarded as piecewise exponential. Such smoothed data can then be incorporated into deconvolution procedures to recover the distortions from the electrode time constant. Higher precision spectrophotometers with increasingly sophisticated computerized data acquisition and noise reduction techniques may allow the E values as well as the Adair constants to be better defined. Work at high concentrations will require special cells for multiple path lengths with O2 electrode or optical sensing of O2 concentration.

Original languageEnglish (US)
Pages (from-to)606-632
Number of pages27
JournalMethods in enzymology
Volume232
Issue numberC
DOIs
StatePublished - Jan 1 1994

Fingerprint

Electrodes
Hemoglobins
Oxygen
Wavelength
Myoglobin
Spectrophotometers
Deconvolution
Noise abatement
Splines
Noise
Data acquisition
Gases
Sensors

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Effects of wavelength on fitting Adair constants for binding of oxygen to human hemoglobin. / Parkhurst, Lawrence J; Larsen, T. M.; Lee, H. Y.

In: Methods in enzymology, Vol. 232, No. C, 01.01.1994, p. 606-632.

Research output: Contribution to journalArticle

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