Crossref journal-article
SAGE Publications
Applied Spectroscopy (179)
Abstract

Myoglobin is an important intracellular protein found in cardiac and skeletal muscle. It is involved in the intracellular transport of oxygen from the cell membrane to the mitochondria where oxidative phosphorylation takes place. The optical absorbance characteristics of myoglobin are similar to those of hemoglobin in the near-infrared spectral region. Distinguishing spectral information of myoglobin from hemoglobin should allow for determination of intracellular oxygen availability in muscle. Partial least-squares analysis is used in this report to determine the oxygen saturation of myoglobin, in the presence of hemoglobin, in vitro. Studies were performed with the use of both transmission and reflectance spectroscopic techniques. Transmission spectra of myoglobin solutions were determined with varying degrees of oxygen saturation achieved by deoxygenating the solution using E. coli. Calibration spectral data sets were developed with the use of varying concentrations of hemoglobin interference, and with varying degrees of myoglobin oxygen saturation. Reflectance spectra were obtained from myoglobin and hemoglobin solutions containing a scattering agent to mimic muscle tissue conditions. Predicted myoglobin saturation values were within 2% of the known saturation values from the use of this analysis. Partial least-squares analysis allows for accurate prediction of myoglobin oxygen saturation in the presence of hemoglobin from either transmission of reflectance near-infrared spectra.

Bibliography

Schenkman, K. A., Marble, D. R., Feigl, E. O., & Burns, D. H. (1999). Near-Infrared Spectroscopic Measurement of Myoglobin Oxygen Saturation in the Presence of Hemoglobin Using Partial Least-Squares Analysis. Applied Spectroscopy, 53(3), 325–331.

Authors 4
  1. Kenneth A. Schenkman (first)
  2. David R. Marble (additional)
  3. Eric O. Feigl (additional)
  4. David H. Burns (additional)
References 13 Referenced 42
  1. 10.1152/jappl.1997.82.1.86
  2. 10.1366/0003702963905763
  3. 10.1117/12.44189
  4. 10.1364/AO.36.002286
  5. {'volume-title': 'Spectrophotometry of Haemoglobin Derivatives', 'year': '1970', 'author': 'Van Assendelft O. W.', 'key': 'bibr5-0003702991946532'} / Spectrophotometry of Haemoglobin Derivatives by Van Assendelft O. W. (1970)
  6. 10.1117/12.180744
  7. 10.1152/jappl.1993.74.5.2194
  8. Kagan L., Myoglobin: Biochemical, Physiological, and Clinical Aspects (Columbia University Press, New York, 1973), p. 9.
  9. 10.1152/physrev.1983.63.1.1
  10. 10.1364/AO.33.001279
  11. {'volume-title': 'Chemometrics', 'year': '1986', 'author': 'Sharaf M. A.', 'key': 'bibr11-0003702991946532'} / Chemometrics by Sharaf M. A. (1986)
  12. 10.1021/ac00162a020
  13. 10.1366/0003702924123412
Dates
Type When
Created 21 years, 10 months ago (Oct. 17, 2003, 12:32 p.m.)
Deposited 5 months, 2 weeks ago (March 11, 2025, 12:53 a.m.)
Indexed 3 months, 1 week ago (May 20, 2025, 6:51 a.m.)
Issued 26 years, 5 months ago (March 1, 1999)
Published 26 years, 5 months ago (March 1, 1999)
Published Online 26 years, 5 months ago (March 1, 1999)
Published Print 26 years, 5 months ago (March 1, 1999)
Funders 0

None

@article{Schenkman_1999, title={Near-Infrared Spectroscopic Measurement of Myoglobin Oxygen Saturation in the Presence of Hemoglobin Using Partial Least-Squares Analysis}, volume={53}, ISSN={1943-3530}, url={http://dx.doi.org/10.1366/0003702991946532}, DOI={10.1366/0003702991946532}, number={3}, journal={Applied Spectroscopy}, publisher={SAGE Publications}, author={Schenkman, Kenneth A. and Marble, David R. and Feigl, Eric O. and Burns, David H.}, year={1999}, month=mar, pages={325–331} }