Paper
1 May 2002 Cytochrome c oxidation determined by multiwavelength optical spectral analysis in the isolated perfused heart
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Abstract
Optical spectroscopy has previously ben used to investigate mitochondrial function in muscle, but spectral overlap of the absorbing species in muscle has limited the accuracy of these determinations. This report demonstrates a multispectral approach to determine cytochrome c redox state in the isolated perfused heart using partial least squares analysis. Optical spectra were acquired in the visible region from the surface of the isolated perfused guinea pig heart and interpreted using reference spectra obtained from in vitro solutions. Calibration spectra were acquired form separate light scattering solutions that contained cytochrome c or myoglobin in both oxidized and reduced states. Cytochrome c redox state and myoglobin oxygen saturation were determined separately form each spectrum obtained form 16 guinea pig hearts during baseline perfusion with oxygenated buffer, during 90 seconds of ischemia and during recovery following the ischemic period. A brief delay between myoglobin deoxygenation and cytochrome c reduction was determined, demonstrating that both processes could be determined simultaneously form the same spectra. This approach may lead to improved determinations of mitochondrial function in the isolated perfused heart.
© (2002) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Kenneth A. Schenkman M.D. "Cytochrome c oxidation determined by multiwavelength optical spectral analysis in the isolated perfused heart", Proc. SPIE 4613, Optical Biopsy IV, (1 May 2002); https://doi.org/10.1117/12.465256
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Cited by 2 scholarly publications.
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KEYWORDS
Heart

Calibration

Oxygen

Spectral calibration

Oxidation

In vitro testing

Error analysis

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