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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">pmj</journal-id><journal-title-group><journal-title xml:lang="ru">Тихоокеанский медицинский журнал</journal-title><trans-title-group xml:lang="en"><trans-title>Pacific Medical Journal</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1609-1175</issn><publisher><publisher-name>TGMU</publisher-name></publisher></journal-meta><article-meta><article-id custom-type="elpub" pub-id-type="custom">pmj-824</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОРИГИНАЛЬНЫЕ ИССЛЕДОВАНИЯ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>ORIGINAL RESEARCHES</subject></subj-group></article-categories><title-group><article-title>Сравнительная свинецсвязывающая активность пектинов с различной молекулярной массой in vitro</article-title><trans-title-group xml:lang="en"><trans-title>COMPARATIVE LEAD-BINDING ACTIVITY OF PECTINS WITH DIFFERENT MOLECULAR MASS IN VITRO</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Макарова</surname><given-names>К. Е.</given-names></name><name name-style="western" xml:lang="en"><surname>Makarova</surname><given-names>K. E.</given-names></name></name-alternatives><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Хожаенко</surname><given-names>Е. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Khozhaenko</surname><given-names>E. V.</given-names></name></name-alternatives><email xlink:type="simple">betula.vl@gmail.com</email><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Хотимченко</surname><given-names>Р. Ю.</given-names></name><name name-style="western" xml:lang="en"><surname>Khotimchenko</surname><given-names>R. Yu.</given-names></name></name-alternatives><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-3"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Ковалев</surname><given-names>В. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Kovalev</surname><given-names>V. V.</given-names></name></name-alternatives><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-3"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Тихоокеанский государственный медицинский университет</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Pacific State Medical University</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>Школа биомедицины Дальневосточного федерального университета; Институт биологии моря им. А.В. Жирмунского ДВО РАН</institution><country>Россия</country></aff><aff xml:lang="en"><institution>School of Biomedicine of the Far Eastern Federal University; A.V. Zhirmunsky Institute of Marine Biology of the Far Eastern Branch of the Russian Academy of Sciences</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru"><institution>Институт биологии моря им. А.В. Жирмунского ДВО РАН</institution><country>Россия</country></aff><aff xml:lang="en"><institution>A.V. Zhirmunsky Institute of Marine Biology of the Far Eastern Branch of the Russian Academy of Sciences</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2013</year></pub-date><pub-date pub-type="epub"><day>28</day><month>06</month><year>2013</year></pub-date><volume>0</volume><issue>2</issue><fpage>85</fpage><lpage>88</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Макарова К.Е., Хожаенко Е.В., Хотимченко Р.Ю., Ковалев В.В., 2013</copyright-statement><copyright-year>2013</copyright-year><copyright-holder xml:lang="ru">Макарова К.Е., Хожаенко Е.В., Хотимченко Р.Ю., Ковалев В.В.</copyright-holder><copyright-holder xml:lang="en">Makarova K.E., Khozhaenko E.V., Khotimchenko R.Y., Kovalev V.V.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.tmj-vgmu.ru/jour/article/view/824">https://www.tmj-vgmu.ru/jour/article/view/824</self-uri><abstract><p>Описана кинетика связывания ионов свинца низкоэтерифицированными пектинами с различными молекулярными массами, полученными методом кислотного гидролиза. Определены показатели максимальной металлсвязывающей активности исследуемых пектиновых образцов в диапазоне рН среды от 2 до 6. Для описания изотерм сорбции и вычисления сорбционных показателей была применена сорбционная модель Лэнгмюра. Установлено, что с уменьшением молекулярной массы пектинов максимальная сорбционная емкость достоверно увеличивается, а сродство пектина к ионам свинца уменьшается.</p></abstract><trans-abstract xml:lang="en"><p>The paper describes kinetics of binding of lead ions with low-etherized pectins with different molecular masses determined by means of acid hydrolysis. The authors have determined indices of maximum metal-binding activity of the pectin specimen under study with the environmental pH range of 2 to 6. The Langmuir adsorption model was used to describe adsorption isotherms and calculate adsorption parameters. As reported, as the molecular mass of pectins reduces, the maximum adsorption capacity reliably increases and the affinity of pectin to lead ions decreases.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>сорбция</kwd><kwd>пектины</kwd><kwd>свинец</kwd></kwd-group><kwd-group xml:lang="en"><kwd>adsorption</kwd><kwd>pectins</kwd><kwd>lead</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Хотимченко Ю.С., Кропотов А.В. Хотимченко М.Ю. Фармакологические свойства пектинов // Эфферентная терапия. 2001. Т. 7, №4. С. 22-36.</mixed-citation><mixed-citation xml:lang="en">Хотимченко Ю.С., Кропотов А.В. Хотимченко М.Ю. Фармакологические свойства пектинов // Эфферентная терапия. 2001. Т. 7, №4. С. 22-36.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Хотимченко Ю.С., Ермак И.М., Бедняк А.Е. и др. 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