Quantitation of heme proteins from spectra of mixtures

Boyle, Rowena C.; Tappel, Al L.; Tappel, Ardelle A.; Chen, Hao

doi:10.1021/jf00037a016

Cited by 17 publications

(7 citation statements)

References 21 publications

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“…Adjustments of extinction coefficients for different Mb forms may be necessary when pH is varied (11). Hemichromes must also be accounted for when present (14). The presence of hemichrome can be assessed by adding excess dithionite to Mb buffered at pH 8, which will result in hemochrome spectra with a large peak at 560 nm (Table 1) if the nonreduced sample was a hemichrome.…”

Section: Practical Considerationsmentioning

confidence: 99%

Redox Reactions of Myoglobin

Richards

2013

Antioxidants & Redox Signaling

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Significance: Failure to maintain myoglobin (Mb) in the reduced state causes the formation of metMb, ferryl Mb species, and cross-linked Mb. Dissociation of ferriprotoporphyrin IX from the globin and release of iron atoms can also occur as oxidized Mb accumulates. These modifications may contribute to various oxidative pathologies in muscle and muscle foods. Recent Advances: The mechanism of ferryl Mb-mediated oxidative damage to nearby structures has been partially elucidated. Dissociation of ferriprotoporphyrin IX from metMb occurs more readily at acidic pH values. The dissociated ferriprotoporphyrin IX (also called hemin) readily decomposes preformed lipid hydroperoxides to reactive oxygen species. Heme oxygenase as well as lipophilic free radicals can degrade the protoporphyrin IX moiety, which results in the formation of free iron. Critical Issues: The multiple pathways by which Mb can incur toxicity create difficulties in determining the major cause of oxidative damage in a particular system. Peroxides and low pH activate each of the oxidative Mb forms, ferriprotoporphyrin IX, and released iron. Determining the relative concentration of these species is technically difficult, but essential to a complete understanding of oxidative pathology in muscle tissue. Future Directions: Improved methods to assess the different pathways of Mb toxicity are needed. Although significant advances have been made in the understanding of Mb interactions with other biomolecules, further investigation is needed to understand the physical and chemical nature of these interactions.

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Section: Practical Considerationsmentioning

confidence: 99%

Redox Reactions of Myoglobin

Richards

2013

Antioxidants & Redox Signaling

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“…tory is a method of deconvoluting composite spectra (500 to 640 nm) and obtaining molar ratio values of heme proteins in tissue samples (1). This heme protein spectral analysis program, measuring reversible and In biological systems some oxidative events are beneirreversible damage to heme proteins, uses a spreadficial, such as the detoxification of xenobiotics, whereas sheet program that analyzes absorbancies at many others are disastrous, e.g., the uncontrolled peroxidapoints in the spectrum rather than a few wavelengths tion of membrane lipids.…”

Section: The Present Application Hsap and Dsap Providementioning

confidence: 99%

“…Routine hemoglobin measurements often utilize cyanide solutions to conwith respect to wavelength; therefore, a turbidity calculation had been introduced to the heme protein spectral vert hemoglobin to the cyanomethemoglobin derivative (8). Turbidity present in tissue homogenates interferes analysis program (1,2).…”

Section: The Present Application Hsap and Dsap Providementioning

confidence: 99%

Section: The Present Application Hsap and Dsap Providementioning

confidence: 99%

“…1 With the previous pendent fixed parameter. This PyrHo method has two advantages, the minimization of interference due to program (1) we could adequately analyze reduced hemoglobin species. However, measurement of oxidized turbidity in tissue homogenates and the vivid illustration of the large amount of hemoglobin present in samheme proteins presented a unique problem in unambiguously assigning individual spectra.…”

Section: The Present Application Hsap and Dsap Providementioning

confidence: 99%

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