Low-temperature impairment of erythrocyte membrane barrier properties – a result of the disorganization of the supramolecular hemoglobin structure
DOI:
https://doi.org/10.15407/dopovidi2015.06.130Keywords:
cryoconservation, cryoprotectants, cryoresistances, erythrocytes, hemoglobinAbstract
Cryoresistances of native erythrocytes and resealed erythrocyte ghosts are compared. It is found that resealed erythrocyte ghosts, where the hemoglobin content is 4–5 times lower than that in erythrocytes, and it is in the form of a molecular solution, are much more cryoresistant than native erythrocytes, which is especially noticeable, when a low concentration of the cryoprotectant (4% glycerol) is used. These data confirm the earlier proposed hypothesis about the role of the supramolecular hemoglobin structure in the mechanism of cryoinjury of erythrocytes.
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References
Lovelock J.E. Biochim. Biophys. Acta., 1953, 10: 414–426. https://doi.org/10.1016/0006-3002(53)90273-X
Ryazantsev V.V. Influence of physical and chemical factors of freezing on spectrin interaction with liposome and erythrocyte membranes: Diss. of cand. of biol. sci., Kharkov, 1990 (in Russian).
Gulevskiy A.K. Barrier-transport properties of plasma membranes during cryopreservation: Diss. of doctor of biol. sci., Kharkov, 1986 (in Russian).
Steck T. L., Kant J.A. Methods Enzymol., 1974, 31: 172–180. https://doi.org/10.1016/0076-6879(74)31019-1
Zhukov A. F., Kolosova I.F., Kuznetsov V.V. Analytical chemistry. Physical and physico-chemical methods of analysis, Moscow: Khimiya, 2001 (in Russian).
Repin N.V., Yurchenko T.N. Topical problems of cryobiology and cryomedicine, Kharkiv, 2012: 165–206 (in Russian).
Trincher K. S. Biology and information (elements of biological thermodynamics), Moscow: Nauka, 1965 (in Russian).
Scherba M.M. Physiology of blood system, Leningrad: Nauka, 1968: 52–93 (in Russian).
Ahlawat S., Chowdhury A., Kumar N., Uppal A., Verma R. S., Gupta P.K. J. Biomed. Opt., 2014, 19, No 8: 087002. https://doi.org/10.1117/1.JBO.19.8.087002
Water and the Cell. Eds. G.H. Pollack, I. L. Cameron, D.N. Wheatley, Berlin: Springer, 2006.
Dzhakson M.B. Molecular and cellular biophysics, Moscow: Mir; BINOM. Laboratoriya znaniy, 2009 (in Russian).
Khabatova B.B., Brazhe H.A., Braze A.P. et al. Abstracts of the V Intern. conf. "Recent Advances in Bionanoscopy", Moscow, June 15–17, 2011: 60–61 (in Russian).
Rozanova Ye.D. Influence of low temperature and cryoprotectants on the structure and function of isolated cytochrome oxidase: Diss. of cand. of biol. sci, Kharkov, 1984 (in Russian).
Solovyova A. S. Calorimetric studies of thermal denaturation of isolated and membrane-bound proteins in the presence of certain cryoprotectant prior to and after cooling to −196 ºC: Diss. of cand. of biol. sci., Kharkov, 1998 (in Russian).
Govorova Yu. S., Zinchenko A.V. Problemy kriobiologii, 2012, 22, No 3: 248 (in Russian).
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