The role of plasmatic erythrocytic membrane in formation of hypoxia in patients with chronic cardiac failure

To study oxygen supply to erythrocytes in patients with chronic cardiac failure as a factor provoking hypoxia. The trial enrolled 12 men with chronic cardiac failure (CCF) of functional NYHA class II aged 37 to 74 years (group A). Group B--healthy donors (n = 10) aged 20-40 years. Conformation chang...

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Published inTerapevtic̆eskii arhiv Vol. 77; no. 9; p. 70
Main Authors Maksimov, G V, Rodnenkov, O V, Luneva, O G, Brazhe, N A, Parshina, E Iu, Rubin, A B, Chazov, E I
Format Journal Article
LanguageRussian
Published Russia (Federation) 2005
Subjects
Adult
Aged
Cardiac Output, Low - complications
Cell Membrane - chemistry
Chronic Disease
Electron Spin Resonance Spectroscopy
Erythrocyte Membrane - chemistry
Erythrocytes - cytology
Hematoporphyrins - chemistry
Hemoglobins - analysis
Hemoglobins - metabolism
Humans
Hypoxia - diagnosis
Hypoxia - etiology
Ligands
Male
Middle Aged
Nitric Oxide - analysis
Oxygen Consumption
Oxyhemoglobins - analysis
Protein Conformation
Viscosity
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Summary:To study oxygen supply to erythrocytes in patients with chronic cardiac failure as a factor provoking hypoxia. The trial enrolled 12 men with chronic cardiac failure (CCF) of functional NYHA class II aged 37 to 74 years (group A). Group B--healthy donors (n = 10) aged 20-40 years. Conformation changes of hemoporphirine were detected with degradation spectroscopy, viscosity of plasmatic membrane--with resonance spectroscopy. Degradation spectroscopy estimated content of Hb-ligant complexes as 0.34 +/- 0.013; complexes I Hb-NO 0.73 +/- 0.11, complexes II Hb-NO 0.28 +/- 0.08 (group A). Electronic-paramagnetic spectroscopy has estimated: S--0.716 +/- 0.005 (group A), 0.667 +/- 0.011 (group B). In group B- 0.5 +/- 0.08; 0.41 +/- 0.22; 0.55 +/- 0.12, respectively. Patients with CHF have high microviscosity of plasmatic erythrocytic membrane near location of polar lipid groups; subnormal content of oxyhemoglobin and elevation of the number of complexes of nitric hemoglobin-oxide; altered binding of nitric oxide with hemoglobin.
ISSN:0040-3660