<?xml version="1.0" encoding="UTF-8"?>
<article xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:noNamespaceSchemaLocation="JATS-archive-oasis-article1-4.xsd" article-type="research-article" dtd-version="1.4" xml:lang="ru">
  <front>
    <journal-meta>
      <journal-title-group>
        <journal-title>Журнал Научное обозрение. Биологические науки</journal-title>
      </journal-title-group>
      <issn>2500-3399</issn>
      <publisher>
        <publisher-name>Общество с ограниченной ответственностью &amp;quot;Издательский Дом &amp;quot;Академия Естествознания&amp;quot;</publisher-name>
      </publisher>
    </journal-meta>
    <article-meta>
      <article-id pub-id-type="publisher-id">ART-1028</article-id>
      <title-group>
        <article-title>НОВЫЙ ПСИХРОФИЛЬНЫЙ КАТЕПСИН L ИЗ ГЕПАТОПАНКРЕАСА КРАСНОГО КОРОЛЕВСКОГО КРАБА (PARALITHODES CAMTSCHATICUS)</article-title>
      </title-group>
      <contrib-group>
        <contrib contrib-type="author">
          <name-alternatives>
            <name xml:lang="ru">
              <surname>Исаев</surname>
              <given-names>В.А.</given-names>
            </name>
          </name-alternatives>
          <name-alternatives>
            <name xml:lang="en">
              <surname>Isaev</surname>
              <given-names>V.A.</given-names>
            </name>
          </name-alternatives>
          <email>trinita@rmt.ru</email>
          <xref ref-type="aff" rid="aff8d4ea977"/>
        </contrib>
        <contrib contrib-type="author">
          <name-alternatives>
            <name xml:lang="ru">
              <surname>Балашова</surname>
              <given-names>M.В.</given-names>
            </name>
          </name-alternatives>
          <name-alternatives>
            <name xml:lang="en">
              <surname>Balashova</surname>
              <given-names>M.V.</given-names>
            </name>
          </name-alternatives>
          <email>trinita@rmt.ru</email>
          <xref ref-type="aff" rid="aff8d4ea977"/>
        </contrib>
        <contrib contrib-type="author">
          <name-alternatives>
            <name xml:lang="ru">
              <surname>Шагин</surname>
              <given-names>Д.</given-names>
            </name>
          </name-alternatives>
          <name-alternatives>
            <name xml:lang="en">
              <surname>Shagin</surname>
              <given-names>D.</given-names>
            </name>
          </name-alternatives>
          <email>trinita@rmt.ru</email>
          <xref ref-type="aff" rid="aff8d4ea977"/>
        </contrib>
        <contrib contrib-type="author">
          <name-alternatives>
            <name xml:lang="ru">
              <surname>Шагина</surname>
              <given-names>И.</given-names>
            </name>
          </name-alternatives>
          <name-alternatives>
            <name xml:lang="en">
              <surname>Shagina</surname>
              <given-names>I.</given-names>
            </name>
          </name-alternatives>
          <email>trinita@rmt.ru</email>
          <xref ref-type="aff" rid="aff8d4ea977"/>
        </contrib>
        <contrib contrib-type="author">
          <name-alternatives>
            <name xml:lang="ru">
              <surname>Еремеев</surname>
              <given-names>H.Л.</given-names>
            </name>
          </name-alternatives>
          <name-alternatives>
            <name xml:lang="en">
              <surname>Eremeev</surname>
              <given-names>N.L.</given-names>
            </name>
          </name-alternatives>
          <email>trinita@rmt.ru</email>
          <xref ref-type="aff" rid="aff8d4ea977"/>
        </contrib>
        <contrib contrib-type="author">
          <name-alternatives>
            <name xml:lang="ru">
              <surname>Руденская</surname>
              <given-names>Г.Н.</given-names>
            </name>
          </name-alternatives>
          <name-alternatives>
            <name xml:lang="en">
              <surname>Rudenskaya</surname>
              <given-names>G.N.</given-names>
            </name>
          </name-alternatives>
          <email>trinita@rmt.ru</email>
          <xref ref-type="aff" rid="aff8d4ea977"/>
        </contrib>
      </contrib-group>
      <aff id="aff8d4ea977">
        <institution xml:lang="ru">Московский государственный университет</institution>
        <institution xml:lang="en">Moscow State University</institution>
      </aff>
      <pub-date date-type="pub" iso-8601-date="2016-06-01">
        <day>01</day>
        <month>06</month>
        <year>2016</year>
      </pub-date>
      <issue>6</issue>
      <fpage>81</fpage>
      <lpage>89</lpage>
      <permissions>
        <license xlink:href="https://creativecommons.org/licenses/by/4.0/">
          <license-p>This is an open-access article distributed under the terms of the CC BY 4.0 license.</license-p>
        </license>
      </permissions>
      <self-uri content-type="url" hreflang="ru">https://science-biology.ru/ru/article/view?id=1028</self-uri>
      <abstract xml:lang="ru" lang-variant="original" lang-source="author">
        <p>Психрофильные и психотолерантные организмы некоторое время или постоянно живущие при низких температурах продуцируют “cold – adapted” ферменты. Известно, что около 90% биосферы существует при температурах ниже 10°С. На поверхности земли преобладают низкотемпературные условия на арктическом и антарктическом континентах, горных районах и морских водах, которые покрывают 70% этой площади и располагаются ниже 1000 м уровня моря, температура не превышает 5°С. Психрофильные организмы живут при таких низких температурах, при которых большинство других видов не может расти и для выживания они нуждаются в ферментах, способных успешно осуществлять катализ в этих экстремальных условиях. Принято считать, что отличительный признак психрофильных ферментов – более высокая активность при низких и умеренных температурах, чем у аналогичных мезофильных ферментов [1, 2]. Эффективность катализа - kcat/KM и значительное увеличение термолабильности предположительно связаны с большей подвижностью полипептидной цепи.</p>
      </abstract>
      <abstract xml:lang="en" lang-variant="translation" lang-source="translator">
        <p>Psikhrofilny and psychotolerant organisms some time or constantly living at low temperatures produce «cold – adapted» enzymes. It is known that about 90% of the biosphere exist at temperatures below 10 °C. On the Earth’s surface low-temperature conditions on the Arctic and Antarctic continents, mountainous areas and sea waters which cover 70% of this area prevail and lower than 1000 m of sea level are located, temperature doesn’t exceed 5 °C. Psikhrofilny organisms live at such low temperatures at which the majority of other types can’t grow and for survival they need the enzymes capable to successfully perform a catalysis in these extreme conditions. It is considered to be that a distinctive sign the psikhrofilnykh of enzymes – higher activity at low and moderate temperatures, than at similar mesophilic enzymes [1, 2]. Efficiency of a catalysis - kcat/KM and significant increase in thermolability are presumably connected with bigger mobility of a polypeptide chain.</p>
      </abstract>
      <kwd-group xml:lang="ru">
        <kwd>катепсин L</kwd>
        <kwd>психотолерантные организмы</kwd>
        <kwd>коллаген</kwd>
      </kwd-group>
      <kwd-group xml:lang="en">
        <kwd>cathepsin L</kwd>
        <kwd>psychrotophic</kwd>
        <kwd>collagenolytic</kwd>
      </kwd-group>
    </article-meta>
  </front>
  <back>
    <ref-list>
      <ref>
        <note>
          <p>1. Список литературы</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>1. G.Gianese, P.Argos &amp; S.Pascarella, Structural adaptation of enzymes to low temperatures, 2002, 14: 141-148</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>2. J.Gomes,W.Steiner, “The Biocftflytic Pjtential of Extremophiles and Extremophiles”Food Technol. Biothechnol., 2004, 42,(4),223-239</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>3. M.Kuddus, P.W.Ramieke, ’Recent developments in production and biothechnological applications jf cjld-active microbial proteases”, Crit.Rev.Microbiol. 2012, 38, 330-338</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>4. M.Fombacke, M.Clarsund,” Cold-adapted Proteases as an Emerging Class of Therapeutics”,Infect. Dis.Ther., 2013 2 (1), 15-26</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>5. A.M.Shmoilov, G.N.Rudenskaya, V.A.Isaev, A.V.Baydakov, R.D.Zhantiev, O.S.Korsunovskaya, L.V.Ageeva, N.V.Starikova, A comparative study of collagenase complex and new homogeneous collagenase preparations for scar treatment. Journal of drug delivery science and technology, 2006, 16: 285-292</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>6. G.N.Rudenskaya, Y.A.Kislitsin, D.V. Rebrikov, Collagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: cDNA cloning and primary structure of the enzymes, BMC Structural Biology, 2004, 2: 20-24</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>7. A.I.Papisova, S.A.Semenova, Y.A.Kislitsyn, G.N.Rudenskaia, Characteristics of substrate hydrolysis by endopeptidases from the hepatopancreas of the king crab, Bioorg Khim (Mosc), 2008, 34-4:, 479-86</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>8. M.E.McGrath, The lysosomal cysteine proteases, Annu. Rev. Biophys. Biomol. Struct. 1999, 28: 181–204</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>9. Aoki H., Ahsan M.N., Watabe S., “Molecular cloning and functional characterization of crustapain: a distinct cysteine proteinase with unique substrate specificity from northern shrimp Pandalus borealis”, 2003, .J Biochem., 133(6): 799-810</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>10. I.B.Leshchinskaya, E.V.Shakirov, E.L.Itskovitch, N.P.Balaban, A.M.Mardanova, M.R.Sharipova, E.V.Blagova, V.M.Levdikov, I.P.Kuranova, G.N.Rudenskaya, V.M.Stepanov, Glutamyl endopeptidase of Bacillus intermedius strain 3-19. Purification, properties, and crystallization, Biochemistry (Mosc), 1997, 62: 903-908</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>11. L.T. Voyushina, E.Yu. Terent’eva, V.M. Stepanov, The synthesis of chromogenic peptide substrates containing p-nitroanilides of arginine and lysine, catalyzed by proteinases adsorbed on support material, Biomed. Biochim. Acta. 1991, 50: 209-212</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>12. B.F.Erlanger, N.Kokowsky, W.Cohen, The preparation and properties of two new chromogenic substrates of trypsin, Arch. Biochem. Biophys. 1961, 95: 271-288</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>13. R. Jr. Chavira, T.J. Burnett, J.H. Hageman, Assaying proteinases with azocollagene, Anal Biochem. 1984, 136: 446-450</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>14. H.Kirschke, A.A.Kembhavi, P.Bohley and A.J.Barrett, Action of rat liver cathepsin L on collagen and other substrates, Biochem J. 1982, 201-2: 367-72</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>15. S. Al-Jassabi, Purification and characterization of cathepsin L from skeletal muscle of the lizard Agama stellio stellio, Biochemistry (Mosc), 200, 65-8: 959-62</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>16. Boulay C., Van Wormhoudt A., Sellos D., “Cloning and expression of cathepsin L-like proteinases in the hepatopancreas of the shrimp Penaeus vannamei during the intermolt cycle”, 1996, J Comp Physiol B., 1996,166(5): 310-318</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>17. Papisova A.I, Javadov A.S., Rudenskaya Yu. A., Balandina G.N., Zhantiev R.D., Korsunovskaia O.S., Dunaevsky Y.E., Rudenskaya G.N “Novel cathepsin L-like protease from dermestid beetle Dermestes frischii maggot”, Biochimie, 2011, 93 (2): 141-148</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>18. Cristofoletti P.T., Ribeiro A.F., Terra W.R., “The cathepsin L-like proteinases from the midgut of Tenebrio molitor larvae: sequence, properties, immunocytochemical localization and function”, Insect Biochem Mol Biol., 2005, 35(8): 883-901</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>19. Kollien A.H., Waniek P.J., Nisbet A.J., Billingsley P.F., Schaub G.A., “Activity and sequence characterization of two cysteine proteases in the digestive tract of the reduviid bug Triatoma infestans”, Insect Mol Biol., 2004,13(6): 569-79</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>20. Matrsumoto I., Abe K., Arai S., Emori Y., “Functional expression and enzymatic properties of two Sitophilus zeamais cysteine proteinases showing different autolytic processing profiles in vitro”, J Biochem., 1998, 123(4): 693-700</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>21. Kuipers A.G., Jongsma M.A., “Isolation and molecular characterization of cathepsin L-like cysteine protease cDNAs from western flower thrips (Frankliniella occidentalis)”, Comp Biochem Physiol B Biochem Mol Biol., 2004, 139(1): 65-75</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>22. Bown D.P., Wilkinson H.S., Jongsma M.A., Gatehouse J.A., “Characterisation of cysteine proteinases responsible for digestive proteolysis in guts of larval western corn rootworm (Diabrotica virgifera) by expression in the yeast Pichia pastoris”, Insect Biochem Mol Biol., 2004, 34(4): 305-320</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>23. Deraison C., Darboux I., Duportets L., Gorojankina T., Rahb? Y., Jouanin L., “Cloning and characterization of a gut-specific cathepsin L from the aphid Aphis gossypii”, Insect Mol Biol., 2004, 13(2): 165-177</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>24. Laycock M.V., MacKay R.M., Di Fruscio M., Gallant JW., “Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus)”, FEBS Let., 1991, 292(2): 115-20</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>25. Kerrer K.M., Peiffer S.L., DiTomas M.E. “Two distinct gene subfamilies within the family of cysteine protease genes”, Proc. Natl. Acad. Sci. USA, 1993, 90: 3063-3067</p>
        </note>
      </ref>
      <ref>
        <note>
          <p>26. E.Lindskog, I.Svensson, L.H?ggstr?m, A homologue of cathepsin L identified in conditioned medium from Sf9 insect cells, Appl. Microbiol. Biotechnol. 2006, 71: 444-449</p>
        </note>
      </ref>
    </ref-list>
  </back>
</article>
