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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">scbmt</journal-id><journal-title-group><journal-title xml:lang="ru">БИОМЕДИЦИНА</journal-title><trans-title-group xml:lang="en"><trans-title>Journal Biomed</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2074-5982</issn><issn pub-type="epub">2713-0428</issn><publisher><publisher-name>Scientific center of biomedical technologies of Federal Medical and Biological Agency</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.33647/2074-5982-18-2-10-16</article-id><article-id custom-type="elpub" pub-id-type="custom">scbmt-1383</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>МЕТОДЫ И ТЕХНОЛОГИИ БИОМЕДИЦИНСКИХ ИССЛЕДОВАНИЙ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>METHODS AND TECHNOLOGIES OF BIOMEDICAL RESEARCH</subject></subj-group></article-categories><title-group><article-title>Влияние пищеварительного тракта на динамику активности ферментов</article-title><trans-title-group xml:lang="en"><trans-title>Influence of the Digestive Tract on Enzyme Activity</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>Ксенофонтов</surname><given-names>Д. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Ksenofontov</surname><given-names>D. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p> д.б.н., доц.,</p><p> 127550, Российская Федерация, Москва, ул. Тимирязевская, 49 </p></bio><bio xml:lang="en"><p> Dr. Sci. (Biol.), Assoc. Prof.</p><p> 127550, Russian Federation, Moscow, Timiryazevskaya Str., 49 </p></bio><email xlink:type="simple">smu@rgau-msha.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>Ксенофонтова</surname><given-names>А. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Ksenofontova</surname><given-names>A. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p> к.б.н., доц.</p><p> 127550, Российская Федерация, Москва, ул. Тимирязевская, 49 </p></bio><bio xml:lang="en"><p> Cand. Sci. (Biol.), Assoc. Prof </p><p> 127550, Russian Federation, Moscow, Timiryazevskaya Str., 49 </p></bio><email xlink:type="simple">angel-ksen@mail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБОУ ВО «Российский государственный аграрный университет — МСХА имени К.А. Тимирязева»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Russian State Agrarian University — Moscow Timiryazev Agricultural Academy</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>10</day><month>06</month><year>2022</year></pub-date><volume>18</volume><issue>2</issue><fpage>10</fpage><lpage>16</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Ксенофонтов Д.А., Ксенофонтова А.А., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Ксенофонтов Д.А., Ксенофонтова А.А.</copyright-holder><copyright-holder xml:lang="en">Ksenofontov D.A., Ksenofontova A.A.</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://journal.scbmt.ru/jour/article/view/1383">https://journal.scbmt.ru/jour/article/view/1383</self-uri><abstract><p>В эксперименте на кроликах и мини-пигах исследована активность ферментов на уровне пищеварительного тракта. Получены результаты активности ферментов в крови, притекающей и оттекающей от желудка и кишечника кролика. Артериовенозная разница выявила снижение активности лактатдегидрогеназы и амилазы при возрастающей активности щелочной фосфатазы у кроликов. Установлена закономерность изменения активности гамма-глутамилтрансферазы в слизистой оболочке кишечника и во фракциях химуса. В слизистой оболочке стенки тонкого кишечника активность трансферазы снижается в дистальном направлении. Максимальная её активность выявлена в растворимой фракции химуса тонкого кишечника, с характерной динамикой снижения в дистальном направлении. С учётом гидратации гликопротеинов полостной слизи в химусе и его существования в виде своеобразной энтероплазмы предполагается закономерная локализация фермента в энтеральной среде между растворимой и плотной эндогенной фракцией с целью проявления максимальной транспортной активности. Сделано заключение о плазмоформирующей роли пищеварительного тракта в части активности ферментов крови.</p></abstract><trans-abstract xml:lang="en"><p>Enzyme activity at the digestive tract level was experimentally studied on rabbits and mini-pigs. The enzyme activity in the blood flow supplied to and from the rabbit stomach and intestines was assessed. In rabbits, the arteriovenous oxygen difference revealed a decrease in the lactate dehydrogenase and amylase activity under an increase in the alkaline phosphatase activity. A regular dependence in the dynamics of gamma-glutamyl transferase activity in the intestinal mucosa and chyme fractions was established. It was found that gamma-glutamyl transferase activity decreases in the distal direction in the mucosa of the small intestine wall. Its maximum activity was determined in the soluble fraction of the small intestine chyme, with a characteristic decrease in the distal direction. Due to the hydration of the cavitary mucus glycoproteins in the chyme and the existence of the latter in the form of an enteroplasm, the enzyme is assumed to localize in the enteric medium between the soluble and dense endogenous fraction with the purpose of displaying the maximum transport activity. A conclusion was made about the plasma-forming role of the digestive tract in terms of blood enzyme activity.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>кишечник</kwd><kwd>химус</kwd><kwd>кровь</kwd><kwd>фермент</kwd><kwd>амилаза</kwd><kwd>щелочная фосфатаза</kwd><kwd>гамма-глутамилтрансфераза</kwd></kwd-group><kwd-group xml:lang="en"><kwd>intestine</kwd><kwd>chyme</kwd><kwd>blood</kwd><kwd>enzyme</kwd><kwd>amylase</kwd><kwd>alkaline phosphatase</kwd><kwd>gamma-glutamyl transferase</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">Gal’perin I.M., Lazarev P.I., Kostiuchenko L.N., Vladimirova E.S. The practical aspects of research on heterophasic cavitary digestion. Usp. Fiziol. Nauk. 1990;21(3):117–124.</mixed-citation><mixed-citation xml:lang="en">Gal’perin I.M., Lazarev P.I., Kostiuchenko L.N., Vladimirova E.S. 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