1 Ocak 2000 Dergi makalesi Açık Erişim

Gershkovich, AA; Verevka, SV; Kibirev, VK; Demchenko, AP

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/94199</identifier>
  <creators>
    <creator>
      <creatorName>Gershkovich, AA</creatorName>
      <givenName>AA</givenName>
      <familyName>Gershkovich</familyName>
    </creator>
    <creator>
      <creatorName>Verevka, SV</creatorName>
      <givenName>SV</givenName>
      <familyName>Verevka</familyName>
    </creator>
    <creator>
      <creatorName>Kibirev, VK</creatorName>
      <givenName>VK</givenName>
      <familyName>Kibirev</familyName>
    </creator>
    <creator>
      <creatorName>Demchenko, AP</creatorName>
      <givenName>AP</givenName>
      <familyName>Demchenko</familyName>
    </creator>
  </creators>
  <titles>
    <title>Solid-State Conjugation Of Proteins With Hydrophobic Compounds In Non-Denaturing Conditions - I. Acylation Of Proteins By Dansyl Proline Using A Polymeric N-Hydroxysuccinimide Ester</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2000</publicationYear>
  <dates>
    <date dateType="Issued">2000-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/94199</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsVersionOf">10.81043/aperta.94198</relatedIdentifier>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.81043/aperta.94199</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">A method of conjugating protein molecules under native conditions with water-insoluble hydrophobic compounds is developed. It permits very water-insoluble acids to be gently coupled to the primary amines on proteins or other biopolymers. For this purpose we synthesized a polymer (co-polymer of N-hydroxymaleimide and N-vinylpyrrolidone cross-linked by benzidine) which swells equally well in water and in organic solvents. Hydrophobic substances are first activated by esterification to this polymer in organic solvent and then conjugated to protein by acylation in aqueous medium at pH 8.0-8.5. Thus, the contact of native protein with organic co-solvent may be completely avoided. The application of this approach is demonstrated by labeling trypsinogen and plasminogen with dansyl proline. (C) 2000 Elsevier Science B.V. All rights reserved.</description>
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