Biochemical Properties of intramolecularly cross-linked hemoglobin

Azhigirova, M. A.; Vyazova, E. P.; Vashkevich, M. G.; Фетисова, Л. В.; Kontuganov, N. N.; Afonin, N. I.

doi:10.1007/bf00834491

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Hemoglobin Preparation1

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2000

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“…The value of P 50 for modified hemoglobin was 28 mm Hg at pH 7.4, P C o, = 40 mm Hg, 37 °C. The biochemical and functional properties of modified hemoglobin were discussed in [21,22].…”

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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“…The value of P 50 for modified hemoglobin was 28 mm Hg at pH 7.4, P C o, = 40 mm Hg, 37 °C. The biochemical and functional properties of modified hemoglobin were discussed in [21,22].…”

Section: Hemoglobin Preparationmentioning

confidence: 99%