Hemoglobin polymers in the animal circulation

Azhigirova, M. A.; Vyazova, E. P.; Vashkevich, M. G.; Nedoshivina, R. V.; Khachatur'yan, A. A.

doi:10.1007/bf00851048

Cited by 2 publications

(2 citation statements)

References 3 publications

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“…14 and pyridoxylated oxyhemoglobin cross-linked by glutaraldehyde (experimental blood substitute) prepared by the method in ref. 15 were kindly given by the Hematological Scientific Center (Moscow). These samples were prepared in solution and stored at liquid nitrogen temperature and in lyophilized form and stored at À20 C. Deoxygenated hemoglobin solutions were prepared by adding Na 2 S 2 O 4 and frozen using liquid nitrogen.…”

Section: Experimental Materialsmentioning

confidence: 99%

Mössbauer spectroscopy in biomedical research

Оштрах¹

2004

Faraday Discuss.

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This work discusses the main directions and results of the application of Mössbauer spectroscopy of iron containing species in biomedical research. These studies demonstrate the wide possibilities of Mössbauer spectroscopy to obtain physical parameters and information about the iron electronic structure in normal and pathological biomolecules, model compounds and pharmaceutical samples as well as about qualitative and quantitative changes of iron containing biomolecules during pathological processes or the effect of environmental factors. The results obtained may be useful for further understanding of the molecular nature of diseases and pathological processes.

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Section: Experimental Materialsmentioning

confidence: 99%

Mössbauer spectroscopy in biomedical research

Оштрах¹

2004

Faraday Discuss.

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“…The hemoglobin solution was dialyzed and concentrated to 8-10 g% of hemoglobin and then stabilized with glucose, sorbitol, etc. Details of the hemoglobin modification were given in [20]. The methemoglobin concentration in solution was measured with an IL 282 Co-oxymeter and found to be 5%.…”

Section: Hemoglobin Preparationmentioning

confidence: 99%

Variation of Quadrupole Splitting in Modified Oxyhemoglobin: A Mössbauer Effect Study

Оштрах¹,

Milder

Semionkin

et al. 2000

Zeitschrift Für Naturforschung A

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Human adult hemoglobin modified by both pyridoxal-5'-phosphate and glutaraldehyde in the oxy-form was studied by Mössbauer spectroscopy. Mössbauer spectra were measured at 87 and 295 K (hemoglobin in lyophilized form) and at 87 K (hemoglobin in frozen solution). The values of the quadrupole splitting for modified oxyhemoglobin were found to be lower then those of oxyhemoglobin without modifications in lyophilized form and frozen solution, respectively. The Mössbauer spectra of modified oxyhemoglobin were also analyzed in terms of the heme iron inequivalence in α-and β-subunits of the tetramer. Differences of the tendencies of temperature dependencies of quadrupole splitting for modified and non-modified oxyhemoglobin in lyophilized form were shown.

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Hemoglobin polymers in the animal circulation

Cited by 2 publications

References 3 publications

Mössbauer spectroscopy in biomedical research

Mössbauer spectroscopy in biomedical research

Variation of Quadrupole Splitting in Modified Oxyhemoglobin: A Mössbauer Effect Study

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