Characterization of the heme iron in pyridoxylated hemoglobin cross- linked by glutaraldehyde using Mossbauer spectroscopy / Oshtrakh M.I., Milder O.B., Semionkin V.A., Berkovsky A.L., Azhigirova M.A., Vyazova E.P. // International Journal of Biological Macromolecules. - 2000. - V. 28, l. 1. - P. 51-58.

ISSN:

01418130

Type:

Article

Abstract:

The heme iron in human adult hemoglobin modified by both pyridoxal-5'- phosphate and glutaraldehyde was characterized by Mossbauer spectroscopy and compared with non-modified hemoglobin. Mossbauer spectra of the samples were measured at 87 and 295 K (1yophilized form) and at 87 K (frozen solution). The values of quadrupole splitting for the oxy-form of modified hemoglobin were found to be lower than those of the oxy-form of hemoglobin without modifications in lyophilized form and frozen solution, respectively. On the other hand, the values of quadrupole splitting for the deoxy-form of modified and non-modified hemoglobins in frozen solution were the same. The Mossbauer spectra of the oxy-form of modified hemoglobin were also analyzed in terms of the heme iron non-equivalence in α- and β-subunits of tetramer. The differences of the tendencies of temperature dependencies of quadrupole splitting for the oxy-form of modified and non-modified hemoglobins in lyophilized form were shown. These results indicated that the heme iron electronic structure and stereochemistry were changed in the oxy-form of pyridoxylated hemoglobin cross-linked by glutaraldehyde. (C) 2000 Elsevier Science B.V.

Author keywords:

Glutaraldehyde; Heme iron electronic structure and stereochemistry; Hemoglobin; Mossbauer spectroscopy; Pyridoxal-5'-phosphate

Index keywords:

deoxyhemoglobin; glutaraldehyde; hemoglobin; hemoprotein; oxyhemoglobin; pyridoxal 5 phosphate; article; cross linking; human; human cell; Mossbauer spectroscopy; oxidation; oxygenation; protein analy

DOI:

10.1016/S0141-8130(00)00142-2

Смотреть в Scopus:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034633766&doi=10.1016%2fS0141-8130%2800%2900142-2&partnerID=40&md5=45b9c2034b7d9439755411adce43d43a

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Поле	Значение
Link	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034633766&doi=10.1016%2fS0141-8130%2800%2900142-2&partnerID=40&md5=45b9c2034b7d9439755411adce43d43a
Affiliations	Division of Applied Biophysics, Fac. Phys. Tech./Devices Qual. Ctrl., Ural State Technical University, Ekaterinburg 620002, Russian Federation; Faculty of Experimental Physics, Ural State Technical University, Ekaterinburg 620002, Russian Federation; HSCRAS, Moscow 125167, Russian Federation
Author Keywords	Glutaraldehyde; Heme iron electronic structure and stereochemistry; Hemoglobin; Mossbauer spectroscopy; Pyridoxal-5'-phosphate
Chemicals/CAS	glutaraldehyde, 111-30-8, 37245-61-7; hemoglobin, 9008-02-0; oxyhemoglobin, 9061-63-6; pyridoxal 5 phosphate, 54-47-7; Cross-Linking Reagents; deoxyhemoglobin, 9008-02-0; Glutaral, 111-30-8; Heme, 14875-96-8; Hemoglobins; Iron, 7439-89-6; Oxygen, 7782-44-7; Oxyhemoglobins; Pyridoxal Phosphate, 54-47-7
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Correspondence Address	Oshtrakh, M.I.; Division of Applied Biophysics, Faculty of Physical Techniques, Ural State Technical University, Ekaterinburg 620002, Russian Federation; email: oshtrakh@soek.erl.e-burg.ru
CODEN	IJBMD
PubMed ID	11033177
Language of Original Document	English
Abbreviated Source Title	Int. J. Biol. Macromol.
Source	Scopus