Change in the parameters of the ultrafine structure of the Mössbauer spectra of oxyhaemoglobin in leukaemias / Oshtrakh M.I., Semenkin V.A. // Biophysics. - 1987. - V. 32, l. 2. - P. 211-217.

ISSN:

00063509

Type:

Article

Abstract:

The parameters of the Mössbauer spectra of oxyhaemoglobin (HbO2) of healthy persons and patients with leukaemia have been evaluated. Rise in quadrupole splitting (ΔEQ) and the isomer shift (δ) of HbO2 was recorded for the patients. Within the approximation made these are linked with change in the energy spectrum of the ground and low-lying electron states of Fe2+ and fall in the total electron density on the 57Fe nucleus, in the main, as a result of change in the Fe2+ bonds with axial ligands. © 1988.

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https://www.scopus.com/inward/record.uri?eid=2-s2.0-45949126041&partnerID=40&md5=1958bccd0b16a44488208d62d902b810

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Поле	Значение
Link	https://www.scopus.com/inward/record.uri?eid=2-s2.0-45949126041&partnerID=40&md5=1958bccd0b16a44488208d62d902b810
Affiliations	Kirov Polytechnic Institute of the Urals, Sverdlovsk, Russian Federation
Correspondence Address	Oshtrakh, M.I.; Kirov Polytechnic Institute of the Urals, Sverdlovsk, Russian Federation
Language of Original Document	English
Abbreviated Source Title	Biophysics
Source	Scopus