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 <front>
  <journal-meta>
   <journal-id journal-id-type="publisher-id">Russian Journal of Biological Physics and Chemisrty</journal-id>
   <journal-title-group>
    <journal-title xml:lang="en">Russian Journal of Biological Physics and Chemisrty</journal-title>
    <trans-title-group xml:lang="ru">
     <trans-title>АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ</trans-title>
    </trans-title-group>
   </journal-title-group>
   <issn publication-format="print">2499-9962</issn>
  </journal-meta>
  <article-meta>
   <article-id pub-id-type="publisher-id">54266</article-id>
   <article-categories>
    <subj-group subj-group-type="toc-heading" xml:lang="ru">
     <subject>МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ</subject>
    </subj-group>
    <subj-group subj-group-type="toc-heading" xml:lang="en">
     <subject>MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY</subject>
    </subj-group>
    <subj-group>
     <subject>МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ</subject>
    </subj-group>
   </article-categories>
   <title-group>
    <article-title xml:lang="en">OXIDATIVE MODIFICATION OF ERYTHROCYTES MODERATELY DOSES OF SODIUM NITRITE in vitro TESTS</article-title>
    <trans-title-group xml:lang="ru">
     <trans-title>ОКИСЛИТЕЛЬНАЯ МОДИФИКАЦИЯ ЭРИТРОЦИТОВ УМЕРЕННЫМИ ДОЗАМИ НИТРИТОМ НАТРИЯ В ОПЫТАХ in vitro</trans-title>
    </trans-title-group>
   </title-group>
   <contrib-group content-type="authors">
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Гусейнова</surname>
       <given-names>С Я</given-names>
      </name>
      <name xml:lang="en">
       <surname>Huseynova</surname>
       <given-names>S Ya</given-names>
      </name>
     </name-alternatives>
     <xref ref-type="aff" rid="aff-1"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Гусейнов</surname>
       <given-names>Т М</given-names>
      </name>
      <name xml:lang="en">
       <surname>Huseynov</surname>
       <given-names>T M</given-names>
      </name>
     </name-alternatives>
     <email>thuseynov@physics.ab.az</email>
     <xref ref-type="aff" rid="aff-2"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Дадашов</surname>
       <given-names>М З</given-names>
      </name>
      <name xml:lang="en">
       <surname>Dadashov</surname>
       <given-names>M Z</given-names>
      </name>
     </name-alternatives>
     <xref ref-type="aff" rid="aff-3"/>
    </contrib>
   </contrib-group>
   <aff-alternatives id="aff-1">
    <aff>
     <institution xml:lang="ru">Институт Биофизики, НАН Азербайджана</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Institute of Biophysics, NAS of Azerbaijan</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-2">
    <aff>
     <institution xml:lang="ru">Институт Биофизики, НАН Азербайджана</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Institute of Biophysics, NAS of Azerbaijan</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-3">
    <aff>
     <institution xml:lang="ru">Институт Биофизики, НАН Азербайджана</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Institute of Biophysics, NAS of Azerbaijan</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <pub-date publication-format="print" date-type="pub" iso-8601-date="2018-03-25T20:22:29+03:00">
    <day>25</day>
    <month>03</month>
    <year>2018</year>
   </pub-date>
   <pub-date publication-format="electronic" date-type="pub" iso-8601-date="2018-03-25T20:22:29+03:00">
    <day>25</day>
    <month>03</month>
    <year>2018</year>
   </pub-date>
   <volume>3</volume>
   <issue>1</issue>
   <fpage>189</fpage>
   <lpage>195</lpage>
   <history>
    <date date-type="received" iso-8601-date="2018-03-20T20:22:29+03:00">
     <day>20</day>
     <month>03</month>
     <year>2018</year>
    </date>
    <date date-type="accepted" iso-8601-date="2018-03-20T20:22:29+03:00">
     <day>20</day>
     <month>03</month>
     <year>2018</year>
    </date>
   </history>
   <self-uri xlink:href="https://rusjbpc.ru/en/nauka/article/54266/view">https://rusjbpc.ru/en/nauka/article/54266/view</self-uri>
   <abstract xml:lang="ru">
    <p>В работе изучена влияния умеренно-хронических доз нитрита натрия на окислительной модификации Hb и эритроцитов, изменения активности каталазы, глутатионпероксидазы (ГП) и интенсивность перекисное окисления липидов (ПОЛ). Анализ спектральных линий раман спектроскопии показывает, что способность Hb связывать кислород I1580/I1548 в суспензии эритроцитов, обработанных NaNO2 существенно выше, чем в контроле и этот эффект прямо зависит от концентрации NaNO2 и значителен уже при минимальных концентрациях NaNO2 (0,07 мМ), а относительное способность Hb отдавать лиганды I1375/I1580 также зависим от дозы, но в противоположную сторону. Проявления симметричных и асимметричных колебаний пиррольных колец Hb (I1375/I1172) с увеличением дозы нитрита повышается на ~ 14 %, что указывает о наличие конформационных изменений пиррольных колец, связанных с окислительной модификацией Hb. Накопление metHb также зависим от от дозы и достигает своего максимума на 30-40 минутах, это сопровождается интенсификацией процессов ПОЛ и увеличением доли мембрансвязаного Hb. Характерно, что развитие окислительного процесса сопровождается уменьшением активности каталазы, а активность ГП изменяется неоднозначно и при повышенных содержаниях NaNO2 несколько растет. Констатируя указанных фактов можно сказать, что уже относительно малые концентрации нитрита натрия могут влиять на конформацию Hb, приводящую к изменению его сродства к О2. Это стимулирует окислительную модификацию Hb, что отражается в росте накопления metHb и потери активности каталазы и ГП, а при больших концентрациях нитрита и к росту активности ГП.</p>
   </abstract>
   <trans-abstract xml:lang="en">
    <p>The work explored the influence of moderately chronic doses of NaNO2 on the oxidative modification of Hb and RBC, changes the activity of catalase, glutathione peroxidase (GP) and the intensity of peroxide oxidation of lipids (LPO). Analysis of the spectral lines of Raman Spectroscopy shows that the ability of the Hb to bind O2 I1580/I1548 in a suspension of erythrocytes treated with NaNO2 is significantly higher than control and this effect directly depends on the concentration of NaNO2 and significant even at the minimum concentrations of NaNO2 (0,07 mm), and relative ability of Hb to give ligands I1375/I1580 is also dose dependent but in the opposite direction. Manifestations of symmetrical and asymmetrical vibrations of the pyrrole rings of Hb (I1375/I1172) increase with an increasing nitrite dose by ~ 14 %, which indicates the presence of conformational changes in the pyrrole rings associated with the oxidative modification of Hb. MetHb accumulation also dose-depend and reaches its maximum at 30-40 minutes, this is accompanied by the intensification of processes of LPO and the increasing share of membrane bound Hb. It is characteristic that the development of oxidative process is accompanied by a decrease in catalase activity and the activity of GP changes ambiguously and multiple grows with increased NaNO2 contents. Noting these facts, we can say that the already relatively small concentrations of nitrite of sodium can affect the conformation of Hb, resulting in a change in his affinity for O2. This stimulates oxidative modification of Hb, which is reflected in the increasing accumulation of metHb and loss of activities of catalase and GP, and at high concentrations of nitrite to increase the activity of GP.</p>
   </trans-abstract>
   <kwd-group xml:lang="ru">
    <kwd>эритроциты</kwd>
    <kwd>гемоглобин</kwd>
    <kwd>каталаза</kwd>
    <kwd>глутатионпероксидаза</kwd>
    <kwd>ПОЛ</kwd>
    <kwd>нитрит натрия</kwd>
   </kwd-group>
   <kwd-group xml:lang="en">
    <kwd>erythrocytes</kwd>
    <kwd>hemoglobin</kwd>
    <kwd>catalase</kwd>
    <kwd>glutathionperoxidase</kwd>
    <kwd>LPO</kwd>
    <kwd>sodium nitrite</kwd>
   </kwd-group>
  </article-meta>
 </front>
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 <back>
  <ref-list>
   <ref id="B1">
    <label>1.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Mensinga T.T., Gerrit J.A., Speijers J.M. Health Implications of Exposure to Environmental Nitrogenous Compounds. Toxicological Reviews, 2003, vol. 22, iss. 1, pp 41-51.</mixed-citation>
     <mixed-citation xml:lang="en">Mensinga T.T., Gerrit J.A., Speijers J.M. Health Implications of Exposure to Environmental Nitrogenous Compounds. Toxicological Reviews, 2003, vol. 22, iss. 1, pp 41-51.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B2">
    <label>2.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Spagnuolo C., Rinelli P., Coletta M., Chiancone E., Ascoli F., Oxidation reaction of human oxyhemoglobin with nitrite: a reexamination. Biochim Biophys Acta., 1987, vol. 5, no. 911, iss. 1, pp. 59-65.</mixed-citation>
     <mixed-citation xml:lang="en">Spagnuolo C., Rinelli P., Coletta M., Chiancone E., Ascoli F., Oxidation reaction of human oxyhemoglobin with nitrite: a reexamination. Biochim Biophys Acta., 1987, vol. 5, no. 911, iss. 1, pp. 59-65.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B3">
    <label>3.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">May J.M., Zhi-Chao Qu, Li Xia, Charles E.C. Nitrite uptake and metabolism and oxidant stress in human erythrocytes. American Journal of Physiology-Cell Physiology, 2000, v. 279, no. 6, pp 1946-1954</mixed-citation>
     <mixed-citation xml:lang="en">May J.M., Zhi-Chao Qu, Li Xia, Charles E.C. Nitrite uptake and metabolism and oxidant stress in human erythrocytes. American Journal of Physiology-Cell Physiology, 2000, v. 279, no. 6, pp 1946-1954</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B4">
    <label>4.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Zavodnik I.B., Lapshina E.A., Rekawiecka K., Zavodnik L.B., Bartosz G., Bryszewska M. Membrane effects of nitrite-induced oxidation of human red blood cells. Biochim Biophys Acta, 1999, vol. 15, no. 1421, iss. 2, pp. 306-16.</mixed-citation>
     <mixed-citation xml:lang="en">Zavodnik I.B., Lapshina E.A., Rekawiecka K., Zavodnik L.B., Bartosz G., Bryszewska M. Membrane effects of nitrite-induced oxidation of human red blood cells. Biochim Biophys Acta, 1999, vol. 15, no. 1421, iss. 2, pp. 306-16.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B5">
    <label>5.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Widmer C.C., Pereira C.P., Gehrig P., Vallelian F., Schoedon G, Buehler P.W, Schaer D.J. Hemoglobin can attenuate hydrogen peroxide-induced oxidative stress by acting as an antioxidative peroxidase. Antioxid Redox Signal, 2010, vol. 12, no. 2, pp. 185-98.</mixed-citation>
     <mixed-citation xml:lang="en">Widmer C.C., Pereira C.P., Gehrig P., Vallelian F., Schoedon G, Buehler P.W, Schaer D.J. Hemoglobin can attenuate hydrogen peroxide-induced oxidative stress by acting as an antioxidative peroxidase. Antioxid Redox Signal, 2010, vol. 12, no. 2, pp. 185-98.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B6">
    <label>6.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Uskokovich-Markovich S., Jelikich-Stankov M., Holclajtner-Antunovich I., Durdevich P. Raman spectrosopy as a new biochemical diagnostic tool. J. Med. Biochem, 2013, vol. 32, no. 2, pp. 96-103.</mixed-citation>
     <mixed-citation xml:lang="en">Uskokovich-Markovich S., Jelikich-Stankov M., Holclajtner-Antunovich I., Durdevich P. Raman spectrosopy as a new biochemical diagnostic tool. J. Med. Biochem, 2013, vol. 32, no. 2, pp. 96-103.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B7">
    <label>7.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Кэри П. Применение спетроскопии КР и РКР в биохимии. М.: Мир, 1985, 272 с. [Cary P. Application of spetroscopy of the RС and RКC in biochemistry. Moscow: Mir, 1985, 272 p. (in Russ)]</mixed-citation>
     <mixed-citation xml:lang="en">Keri P. Primenenie spetroskopii KR i RKR v biohimii. M.: Mir, 1985, 272 s. [Cary P. Application of spetroscopy of the RS and RKC in biochemistry. Moscow: Mir, 1985, 272 p. (in Russ)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B8">
    <label>8.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Соловьев К.Н., Гладков Л.Л., Старухин А.С. Спектроскопия порфиринов: Колебательные состояния. Минск: Наука и техника, 1985, 415 с. [Soloviev K.N., Gladkov L.L., Starukhin A.S. Spectroscopy of porphyrins: Oscillatory states. Minsk: Science and Technology, 1985, 415 p. (in Russ)]</mixed-citation>
     <mixed-citation xml:lang="en">Solov'ev K.N., Gladkov L.L., Staruhin A.S. Spektroskopiya porfirinov: Kolebatel'nye sostoyaniya. Minsk: Nauka i tehnika, 1985, 415 s. [Soloviev K.N., Gladkov L.L., Starukhin A.S. Spectroscopy of porphyrins: Oscillatory states. Minsk: Science and Technology, 1985, 415 p. (in Russ)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B9">
    <label>9.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Максимов Г.В., Максимова Н.В., Чурие А.А. и др. Исследование изменений конформации порфирина гемоглобина при первичной гипертензии. Биохимия, 2001, т. 66, вып. 3, с. 365-370. [Maksimov G.V., Maksimova N.V., Churie A.A. Research of changes in the conformation of porphyrin hemoglobin in primary hypertension. Biochemistry, 2001, vol. 66, iss. 3, p. 365-370. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Maksimov G.V., Maksimova N.V., Churie A.A. i dr. Issledovanie izmeneniy konformacii porfirina gemoglobina pri pervichnoy gipertenzii. Biohimiya, 2001, t. 66, vyp. 3, s. 365-370. [Maksimov G.V., Maksimova N.V., Churie A.A. Research of changes in the conformation of porphyrin hemoglobin in primary hypertension. Biochemistry, 2001, vol. 66, iss. 3, p. 365-370. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B10">
    <label>10.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Winterbourn C.C. Oxidative reactions of hemoglobin. Methods Enzymol., 1990, vol. 186, pp. 265-272.</mixed-citation>
     <mixed-citation xml:lang="en">Winterbourn C.C. Oxidative reactions of hemoglobin. Methods Enzymol., 1990, vol. 186, pp. 265-272.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B11">
    <label>11.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Szebeni J., Winterbourn C. C., Carrell R. W. Oxidative interactions between haemoglobin and membrane lipid. A liposome model. Biochem. J., 1984, vol. 220, no. 3, pp. 685-692.</mixed-citation>
     <mixed-citation xml:lang="en">Szebeni J., Winterbourn C. C., Carrell R. W. Oxidative interactions between haemoglobin and membrane lipid. A liposome model. Biochem. J., 1984, vol. 220, no. 3, pp. 685-692.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B12">
    <label>12.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Моин В.М. Простой и специфический метод определения активности глутатионперокси-дазы в эритроцитах. Лаб. Дело, 1986, no. 12, c. 724-727. [Moin V.M. A simple and specific method for determining the activity of glutathione peroxydase in erythrocytes. Lab. Delo, 1986, no. 12, pp. 724-727. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Moin V.M. Prostoy i specificheskiy metod opredeleniya aktivnosti glutationperoksi-dazy v eritrocitah. Lab. Delo, 1986, no. 12, c. 724-727. [Moin V.M. A simple and specific method for determining the activity of glutathione peroxydase in erythrocytes. Lab. Delo, 1986, no. 12, pp. 724-727. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B13">
    <label>13.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Королюк М. А. Метод определения активности каталазы. Лаб. дело, 1988, т. 64, № 3, c. 16-17. [Korolyuk M.A. Method for determination of catalase activity. Lab. Delo, 1988, т. 64, no. 3, c. 16-17. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Korolyuk M. A. Metod opredeleniya aktivnosti katalazy. Lab. delo, 1988, t. 64, № 3, c. 16-17. [Korolyuk M.A. Method for determination of catalase activity. Lab. Delo, 1988, t. 64, no. 3, c. 16-17. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B14">
    <label>14.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Лакин Г.Ф. Биометрия. М.: Высшая школа, 1990, 352 с. [Lakin G.F. Biometriya. Moscow, 1990, 352 p. (in Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Lakin G.F. Biometriya. M.: Vysshaya shkola, 1990, 352 s. [Lakin G.F. Biometriya. Moscow, 1990, 352 p. (in Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B15">
    <label>15.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Иржак Л.И. Hb и их свойства. М.: Наука, 1975, 239 с. [Irjak L.I. Hb and their properties. Moscow: Nauka, 1975, 352 c. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Irzhak L.I. Hb i ih svoystva. M.: Nauka, 1975, 239 s. [Irjak L.I. Hb and their properties. Moscow: Nauka, 1975, 352 c. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B16">
    <label>16.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Duke researchers discover central role of Nitric Oxide in hemoglobin action. Duke Medicine News and Communication, 2004, vol. 3.</mixed-citation>
     <mixed-citation xml:lang="en">Duke researchers discover central role of Nitric Oxide in hemoglobin action. Duke Medicine News and Communication, 2004, vol. 3.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B17">
    <label>17.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Рубан М.К., Вашанов Г.А., Лавриненко И.А. Структурно-функциональные модификации нитрозилированного Hbа, индуцированные оксигенацией. Вестник ВГУ, Серия: Биология. Фармация, 2010, № 1, с. 56-61. [Ruban M.K, Vashanov G.A, Lavrinenko I.A. Structural and functional modifications of nitrosylated Hba, induced by oxygenation. Digest VSU, Series: Biology. Pharmacia, 2010, no. 1, p. 56-61. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Ruban M.K., Vashanov G.A., Lavrinenko I.A. Strukturno-funkcional'nye modifikacii nitrozilirovannogo Hba, inducirovannye oksigenaciey. Vestnik VGU, Seriya: Biologiya. Farmaciya, 2010, № 1, s. 56-61. [Ruban M.K, Vashanov G.A, Lavrinenko I.A. Structural and functional modifications of nitrosylated Hba, induced by oxygenation. Digest VSU, Series: Biology. Pharmacia, 2010, no. 1, p. 56-61. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B18">
    <label>18.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hobbs A.I., Gladwin M.T., Patel R.P., Williams D.L.H., Butler A.R. Haemoglobin: NO transporter, NO inactivator or NO of the above. TRENDS in Pharmacological Science, 2002, vol. 23, р. 406-411.</mixed-citation>
     <mixed-citation xml:lang="en">Hobbs A.I., Gladwin M.T., Patel R.P., Williams D.L.H., Butler A.R. Haemoglobin: NO transporter, NO inactivator or NO of the above. TRENDS in Pharmacological Science, 2002, vol. 23, r. 406-411.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B19">
    <label>19.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Ramser K, Logg K, Goksör M, Enger J, Käll M, Hanstorp D. Resonance Raman spectroscopy of optically trapped functional erythrocytes. J Biomed Opt., 2004, vol. 9, no. 3, pp. 593-600.</mixed-citation>
     <mixed-citation xml:lang="en">Ramser K, Logg K, Goksör M, Enger J, Käll M, Hanstorp D. Resonance Raman spectroscopy of optically trapped functional erythrocytes. J Biomed Opt., 2004, vol. 9, no. 3, pp. 593-600.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B20">
    <label>20.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Podstawka E, Rajani C, Kincaid JR, Proniewicz LM. Resonance Raman studies of heme structural differences in subunits of deoxyhemoglobin. Biopolymers, 2000, vol. 57, no. 4, pp. 201-207.</mixed-citation>
     <mixed-citation xml:lang="en">Podstawka E, Rajani C, Kincaid JR, Proniewicz LM. Resonance Raman studies of heme structural differences in subunits of deoxyhemoglobin. Biopolymers, 2000, vol. 57, no. 4, pp. 201-207.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B21">
    <label>21.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Tsuneshige A, Imai K, Tyuma I. The binding of hemoglobin to red cell membrane lowers its oxygen affinity. J Biochem., 1987, vol. 101, no. 3, pp. 695-704.</mixed-citation>
     <mixed-citation xml:lang="en">Tsuneshige A, Imai K, Tyuma I. The binding of hemoglobin to red cell membrane lowers its oxygen affinity. J Biochem., 1987, vol. 101, no. 3, pp. 695-704.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B22">
    <label>22.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Kirschner-Zilber I, Setter E, Shaklai N. Association of hemoglobin chains with the cell membrane as a cause of red cell distortion in thalassemia. Biochem Med Metab Biol., 1987, vol. 38, no. 1, no. 19-31.</mixed-citation>
     <mixed-citation xml:lang="en">Kirschner-Zilber I, Setter E, Shaklai N. Association of hemoglobin chains with the cell membrane as a cause of red cell distortion in thalassemia. Biochem Med Metab Biol., 1987, vol. 38, no. 1, no. 19-31.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B23">
    <label>23.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Welbourn E.M, Wilson M.T, Yusof A, Metodiev M.V, Cooper C.E. The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radical Biology and Medicine, 2017, vol. 103, pp. 95-106.</mixed-citation>
     <mixed-citation xml:lang="en">Welbourn E.M, Wilson M.T, Yusof A, Metodiev M.V, Cooper C.E. The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radical Biology and Medicine, 2017, vol. 103, pp. 95-106.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B24">
    <label>24.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Осипов А. Н., Борисенко Г. Г., Владимиров Ю. А. Биологическая роль нитрозильных комплексов гемопротеинов. Успехи биологической химии, 2007, т. 47, с. 259-292. [Osipov A.N., Borisenko G.G., Vladimirov Yu. A. Biological role of nitrosyl complexes of hemoproteins. Uspekhi biologicheskoy khimii, 2007, vol. 47, p. 259-292. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Osipov A. N., Borisenko G. G., Vladimirov Yu. A. Biologicheskaya rol' nitrozil'nyh kompleksov gemoproteinov. Uspehi biologicheskoy himii, 2007, t. 47, s. 259-292. [Osipov A.N., Borisenko G.G., Vladimirov Yu. A. Biological role of nitrosyl complexes of hemoproteins. Uspekhi biologicheskoy khimii, 2007, vol. 47, p. 259-292. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B25">
    <label>25.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Giulivi C, Davies K.J. Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol., 1994, vol. 231, pp. 490-6.</mixed-citation>
     <mixed-citation xml:lang="en">Giulivi C, Davies K.J. Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol., 1994, vol. 231, pp. 490-6.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B26">
    <label>26.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Ansari F.A., Mahmood R. Sodium nitrite enhances generation of reactive oxygen species that decrease antioxidant power and inhibit plasma membrane redox system of human erythrocytes. Cell Biol Int., 2016, vol. 40, vol. 8, pp. 887-894.</mixed-citation>
     <mixed-citation xml:lang="en">Ansari F.A., Mahmood R. Sodium nitrite enhances generation of reactive oxygen species that decrease antioxidant power and inhibit plasma membrane redox system of human erythrocytes. Cell Biol Int., 2016, vol. 40, vol. 8, pp. 887-894.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B27">
    <label>27.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Montenegro M.F., Pinheiro L.C., Amaral J.H., Marçal D.M., Palei A.C., Costa-Filho A.J., Tanus-Santos J.E. Antihypertensive and antioxidant effects of a single daily dose of sodium nitrite in a model of renovascular hypertension. Naunyn Schmiedebergs Arch Pharmacol., 2012, vol. 385, no. 5, no. 509-17.</mixed-citation>
     <mixed-citation xml:lang="en">Montenegro M.F., Pinheiro L.C., Amaral J.H., Marçal D.M., Palei A.C., Costa-Filho A.J., Tanus-Santos J.E. Antihypertensive and antioxidant effects of a single daily dose of sodium nitrite in a model of renovascular hypertension. Naunyn Schmiedebergs Arch Pharmacol., 2012, vol. 385, no. 5, no. 509-17.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B28">
    <label>28.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hogg N., Kalyanaraman B. Nitric oxide and lipid peroxidation. Biochim Biophys Acta., 1999, vol. 1411, no. 2-3, pp. 378-384.</mixed-citation>
     <mixed-citation xml:lang="en">Hogg N., Kalyanaraman B. Nitric oxide and lipid peroxidation. Biochim Biophys Acta., 1999, vol. 1411, no. 2-3, pp. 378-384.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B29">
    <label>29.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Violi F., Marino R., Milite M.T., Loffredo L. Nitric oxide and its role in lipid peroxidation. Diabetes Metab Res Rev., 1999, vol. 15, no. 4, pp. 283-288</mixed-citation>
     <mixed-citation xml:lang="en">Violi F., Marino R., Milite M.T., Loffredo L. Nitric oxide and its role in lipid peroxidation. Diabetes Metab Res Rev., 1999, vol. 15, no. 4, pp. 283-288</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B30">
    <label>30.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Шугалей И.В., Львов С.Н., Целинский И.В., Баев В.И. Влияние интоксикации нитритом натрия на активность ферментов антиоксидантной защиты и процессы пероксидации в эритроцитах мыши. Укр. биохим. журнал, 1992, т. 64, вып. 2, с. 111-114. [Shugaley I.V., Lvov S.N., Tselinsky I.V., Baev V.I. Influence of sodium nitrite intoxication on the activity of antioxidant defense enzymes and peroxidation processes in mouse erythrocytes. Ukr. biochem. Journal, 1992, vol. 64, iss. 2, p. 111-114. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Shugaley I.V., L'vov S.N., Celinskiy I.V., Baev V.I. Vliyanie intoksikacii nitritom natriya na aktivnost' fermentov antioksidantnoy zaschity i processy peroksidacii v eritrocitah myshi. Ukr. biohim. zhurnal, 1992, t. 64, vyp. 2, s. 111-114. [Shugaley I.V., Lvov S.N., Tselinsky I.V., Baev V.I. Influence of sodium nitrite intoxication on the activity of antioxidant defense enzymes and peroxidation processes in mouse erythrocytes. Ukr. biochem. Journal, 1992, vol. 64, iss. 2, p. 111-114. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B31">
    <label>31.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Титов В.Ю., Петренко М.Ю., Взаимодействие нитрита с каталазой как важный элемент его токсичности. Биохимия, 2003, т. 68, вып. 6, с. 769-777. [Titov V.Yu., Petrenko M.Yu., Interaction of nitrite with catalase as an important element of its toxicity. Biochemistry, 2003, vol. 68, iss. 6, pp. 769-777. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Titov V.Yu., Petrenko M.Yu., Vzaimodeystvie nitrita s katalazoy kak vazhnyy element ego toksichnosti. Biohimiya, 2003, t. 68, vyp. 6, s. 769-777. [Titov V.Yu., Petrenko M.Yu., Interaction of nitrite with catalase as an important element of its toxicity. Biochemistry, 2003, vol. 68, iss. 6, pp. 769-777. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B32">
    <label>32.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Titov V.Yu., Osipov A.N. Nitrite and nitroso compounds can serve as specific catalase inhibitors. Redox Report, 2017, vol. 22, no. 2, pp. 91-97.</mixed-citation>
     <mixed-citation xml:lang="en">Titov V.Yu., Osipov A.N. Nitrite and nitroso compounds can serve as specific catalase inhibitors. Redox Report, 2017, vol. 22, no. 2, pp. 91-97.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B33">
    <label>33.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Rocha S., Gomes D., Lima M., Bronze-da-Rocha E., Santos-Silva A. Peroxiredoxin 2, glutathione peroxidase, and catalase in the cytosol and membrane of erythrocytes under H2O2-induced oxidative stress. Free Radic Res., 2015, vol. 49, no. 8, pp. 990-1003.</mixed-citation>
     <mixed-citation xml:lang="en">Rocha S., Gomes D., Lima M., Bronze-da-Rocha E., Santos-Silva A. Peroxiredoxin 2, glutathione peroxidase, and catalase in the cytosol and membrane of erythrocytes under H2O2-induced oxidative stress. Free Radic Res., 2015, vol. 49, no. 8, pp. 990-1003.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B34">
    <label>34.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Asahi M., Fujii J., Suzuki K., Seo H.G., Kuzuya T., Hori M., Tada M., Fujii S., Taniguchi N. Inactivation of glutathione peroxidase by nitric oxide. Implication for cytotoxicity. J Biol Chem., 1995, vol. 270, no. 36, pp. 21035-21039.</mixed-citation>
     <mixed-citation xml:lang="en">Asahi M., Fujii J., Suzuki K., Seo H.G., Kuzuya T., Hori M., Tada M., Fujii S., Taniguchi N. Inactivation of glutathione peroxidase by nitric oxide. Implication for cytotoxicity. J Biol Chem., 1995, vol. 270, no. 36, pp. 21035-21039.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B35">
    <label>35.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Гусейнова С.Я., Гулиева Р.Т., Дадашов М.З., Джафаров А.И., Яхъяева Ф.Р., Гусейнов Т.М. Окислительная модификация гемоглобина изолированных эритроцитов в инкубационной среде, содержащей нитрит натрия и селенит натрия. Вестник Новосибирского государственного пед. ун-та, 2016, т. 5, № 33, с. 207-217. [Huseynova S.Ya., Guliyeva R.T., Dadashov M.Z., Jafarov A.I., Yakhyaeva F.R., Huseynov T.M. Bulletin of the Novosibirsk State Pedagogical University, 2016, vol. 5, no. 33, pp. 207-217. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Guseynova S.Ya., Gulieva R.T., Dadashov M.Z., Dzhafarov A.I., Yah'yaeva F.R., Guseynov T.M. Okislitel'naya modifikaciya gemoglobina izolirovannyh eritrocitov v inkubacionnoy srede, soderzhaschey nitrit natriya i selenit natriya. Vestnik Novosibirskogo gosudarstvennogo ped. un-ta, 2016, t. 5, № 33, s. 207-217. [Huseynova S.Ya., Guliyeva R.T., Dadashov M.Z., Jafarov A.I., Yakhyaeva F.R., Huseynov T.M. Bulletin of the Novosibirsk State Pedagogical University, 2016, vol. 5, no. 33, pp. 207-217. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
  </ref-list>
 </back>
</article>
