Spectrophotometric Determination of the Oxygen Saturation of Whole Blood

Tsao, Makepeace U.; Sethna, Shirley S.; Sloan, Charles H.; Wyngarden, Lillian J.

doi:10.1016/s0021-9258(19)57196-4

Cited by 16 publications

(3 citation statements)

References 9 publications

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“…As expected, the reaction in Fig 1B with dithionite is completed on the order of seconds, the reaction with sodium nitrite is on the order of 1 minute and the reaction with Oxyrase is completed on the order of 5-10 minutes. Overlaid spectra from deoxyHb treated with Oxyrase shows no significant change to the isosbestic point at 505 nm reported in [48]. the solution pH as a function of lactate concentration and volume percent Oxyrase, and supports the conclusions that less lactate, higher pH (closer to the reported optimal pH for Oxyrase at 8.4) results in DO measurements that are near zero [39,47].…”

Section: Reactions With Free Hemoglobin From Healthy Donorssupporting

confidence: 65%

“…For cell-free deoxyHb samples prepared with dithionite and Oxyrase, the percentage of oxyHb and deoxyHb was calculated using the method presented in [48]. A linear correlation of the percentage of oxygen saturation as a function of a ratio of the extinction coefficients ε 575 /ε 505 was obtained by measuring oxygen-saturated Hb and a completely anaerobic sample of deox-yHb.…”

Section: Spectrophotometry Of Hbmentioning

confidence: 99%

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Magnetophoretic and spectral characterization of oxyhemoglobin and deoxyhemoglobin: Chemical versus enzymatic processes

et al. 2021

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A new method for hemoglobin (Hb) deoxygenation, in suspension or within red blood cells (RBCs) is described using the commercial enzyme product, EC-Oxyrase®. The enzymatic deoxygenation method has several advantages over established deoxygenation methodologies, such as avoiding side reactions that produce methemoglobin (metHb), thus eliminating the need for an inert deoxygenation gas and airtight vessel, and facilitates easy re-oxygenation of Hb/RBCs by washing with a buffer that contains dissolved oxygen (DO). The UV-visible spectra of deoxyHb and metHb purified from human RBCs using three different preparation methods (sodium dithionite [to produce deoxyHb], sodium nitrite [to produce metHb], and EC-Oxyrase® [to produce deoxyHb]) show the high purity of deoxyHb prepared using EC-Oxyrase® (with little to no metHb or hemichrome production from side reactions). The oxyHb deoxygenation time course of EC-Oxyrase® follows first order reaction kinetics. The paramagnetic characteristics of intracellular Hb in RBCs were compared using Cell Tracking Velocimetry (CTV) for healthy and sickle cell disease (SCD) donors and oxygen equilibrium curves show that the function of healthy RBCs is unchanged after EC-Oxyrase® treatment. The results confirm that this enzymatic approach to deoxygenation produces pure deoxyHb, can be re-oxygenated easily, prepared aerobically and has similar paramagnetic mobility to existing methods of producing deoxyHb and metHb.

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Section: Reactions With Free Hemoglobin From Healthy Donorssupporting

confidence: 65%

Section: Spectrophotometry Of Hbmentioning

confidence: 99%

Magnetophoretic and spectral characterization of oxyhemoglobin and deoxyhemoglobin: Chemical versus enzymatic processes

et al. 2021

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“…Four more blood samples of different oxygenation levels were prepared by mixing the two stock samples in predetermined volumetric ratios (Scheid and Meyer 1978). As a control, optical sO 2 measurements were made on haemolysed blood samples (0.5% saponin, Sigma-Aldrich) using a spectrophotometer (GENESYS 20, Thermo Electron) in the wavelength range of 700-1000 nm with a step size of 4 nm (Tsao et al 1955). For PA measurements, these blood samples were injected into optically transparent plastic TYGON tubes of 0.25 mm inner diameter, which were immersed in water.…”

Section: Experimental Set-upmentioning

confidence: 99%

Limitations of quantitative photoacoustic measurements of blood oxygenation in small vessels

et al. 2007

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We investigate the feasibility of obtaining accurate quantitative information, such as local blood oxygenation level (sO2), with a spatial resolution of about 50 microm from spectral photoacoustic (PA) measurements. The optical wavelength dependence of the peak values of the PA signals is utilized to obtain the local blood oxygenation level. In our in vitro experimental models, the PA signal amplitude is found to be linearly proportional to the blood optical absorption coefficient when using ultrasonic transducers with central frequencies high enough such that the ultrasonic wavelengths are shorter than the light penetration depth into the blood vessels. For an optical wavelength in the 578-596 nm region, with a transducer central frequency that is above 25 MHz, the sensitivity and accuracy of sO2 inversion is shown to be better than 4%. The effect of the transducer focal position on the accuracy of quantifying blood oxygenation is found to be negligible. In vivo oxygenation measurements of rat skin microvasculature yield results consistent with those from in vitro studies, although factors specific to in vivo measurements, such as the spectral dependence of tissue optical attenuation, dramatically affect the accuracy of sO2 quantification in vivo.

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Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes

et al. 2017

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Gold nanorods (GNRs) are a unique class of metal nanostructures that have attractive potentials in biomedical applications, and the concern on their biological safety is concomitantly increasing. Hemocompatibility is extremely important as their contact with blood circulation is unavoidable during in vivo delivery. Herein, two kinds of GNRs coated with hexadecyltrimethylammonium bromide (C‐GNRs) or poly(sodium‐p‐styrenesulfonate) are used to test their potential toxicological effects in blood. C‐GNRs with positive surface charges efficiently induce hemolysis when encountering erythrocytes. Cellular internalization of C‐GNRs is found, and they subsequently bind with hemoglobin, forming bioconjugates. The interaction between hemoglobin and C‐GNR (stoichiometry 32.7:1) is regulated by electrostatic forces. Chromophores like tryptophan (Trp) are found to interact with C‐GNRs, causing enhancement in fluorescence intensity. The conformation of protein is partially altered, evidenced by decrease in α‐helical, increase in β‐sheet and random coil of hemoglobin. Although C‐GNRs do not essentially decrease oxygen binding capacity of hemoglobin, they hamper oxygen release from the protein. Heme, the oxygen binding unit, releases from hemoglobin upon C‐GNR treatment, which could contribute to C‐GNR‐induced hemolysis. This study demonstrates the hematological effects of GNRs, revealing their potential risk in biomedical applications.

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Spectrophotometric Determination of the Oxygen Saturation of Whole Blood

Cited by 16 publications

References 9 publications

Magnetophoretic and spectral characterization of oxyhemoglobin and deoxyhemoglobin: Chemical versus enzymatic processes

Magnetophoretic and spectral characterization of oxyhemoglobin and deoxyhemoglobin: Chemical versus enzymatic processes

Limitations of quantitative photoacoustic measurements of blood oxygenation in small vessels

Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes

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