Mössbauer and positron annihilation studies of structural modifications of hemoglobin in solution / Oshtrakh M.I., Kopelyan E.A., Semionkin V.A. // Journal of Radioanalytical and Nuclear Chemistry Articles. - 1995. - V. 190, l. 2. - P. 243-249.

ISSN:
02365731
Type:
Article
Abstract:
Structural modifications of human adult oxyhemoglobin in concentrated solution were studied by Mössbauer and positron life-time spectroscopies. The effects of non-sterile degradation and irradiation by γ-rays were compared by both techniques. It was found that positron annihilation parameters were sensitive to the structural modifications of hemoglobin molecules in solution and could be related with the conformational states of hemoglobin. © 1995 Akadémiai Kiadó.
Author keywords:
Index keywords:
hemoglobin; conference paper; gamma irradiation; mossbauer spectroscopy; protein structure
DOI:
10.1007/BF02039999
Смотреть в Scopus:
https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028927640&doi=10.1007%2fBF02039999&partnerID=40&md5=338db423bda1f91dcae48c621cf196e8
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Поле Значение
Link https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028927640&doi=10.1007%2fBF02039999&partnerID=40&md5=338db423bda1f91dcae48c621cf196e8
Affiliations Division of Applied Biophysics, Ural State Technical UniversityI, Sverdlovsk, 620002, Russian Federation; Faculty of Experimental Physics, Ural State Technical UniversityI, Sverdlovsk, 620002, Russian Federation
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Correspondence Address Oshtrakh, M.I.; Division of Applied Biophysics, Ural State Technical UniversityI, Sverdlovsk, 620002, Russian Federation
Publisher Kluwer Academic Publishers
CODEN JRNCD
Language of Original Document English
Abbreviated Source Title Journal of Radioanalytical and Nuclear Chemistry, Articles
Source Scopus