Literature DB >> 16599213

Oxyhemoglobin saturation measurements by green spectral shift.

Kurt R Denninghoff1, Russell A Chipman, Lloyd W Hillman.   

Abstract

From an analysis of new hemoglobin solution transmission spectra at various oxygen saturations (SO2), path lengths, and pH, we find the determination of SO2 by using the classical oximetry technique to be poorly calibrated. We used this data set to develop a proposed method for SO2 determination based on the spectral shift of the hemoglobin transmission minimum between 475 and 510 nm. The method does not require accurate knowledge of hemoglobin extinction coefficients and is linear in relation to SO2 despite changes in path length, pH, or hemoglobin concentration.

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Year:  2006        PMID: 16599213     DOI: 10.1364/ol.31.000924

Source DB:  PubMed          Journal:  Opt Lett        ISSN: 0146-9592            Impact factor:   3.776


  1 in total

1.  Interaction of Normal and Sickle Hemoglobins for Sodium Dodecylsulphate and Hydrogen Peroxide at pH 5.0 and 7.2.

Authors:  Fortunatus C Ezebuo; Sabinus Oscar O Eze; Colin B Lukong; Ferdinand C Chilaka
Journal:  ISRN Hematol       Date:  2013-10-10
  1 in total

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