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Kathepsine C:Een allosterisch enzyme

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  • المؤلفون: Gorter, Jeannette
  • المصدر:
    Gorter , J 1969 , ' Kathepsine C : Een allosterisch enzyme ' , Doctor of Philosophy , Groningen .
  • نوع التسجيلة:
    Electronic Resource
  • الدخول الالكتروني :
    https://research.rug.nl/en/publications/e4ca3d42-d7ee-44a9-a80a-4e353a3b066f
    https://hdl.handle.net/11370/e4ca3d42-d7ee-44a9-a80a-4e353a3b066f
    https://pure.rug.nl/ws/files/14431686/Gorter_J..pdf
  • معلومة اضافية
    • Publisher Information:
      s.n. 1969
    • نبذة مختصرة :
      In chapter I an introduction into allosteric systems is given. In chapter II is a detailed method is described for the applica of Gly-Phe--p. nitroanilide (GPNA) as a substrate for the activity assay of the lysosomal enzyme cathepsin C. It is an allosteric which is activated by Cl-, Br-, 1-, CNS-, NO-3 and ClO3 ions. (Chapter III). At high activator concentrations the enzyme Michaelis-Menten kinetics, at low concentrations there is substrate cooperativity. Thus, in the absence of added activators a small amount of the substrate Ala-Phe-amide enhances the hydrolysis rate of a low concentration of GPKA; at higher concentrations it is a competitive inhibitor.........
    • الموضوع:
    • Availability:
      Open access content. Open access content
      info:eu-repo/semantics/openAccess
    • Note:
      application/pdf
      Dutch
    • Other Numbers:
      GRU oai:pure.rug.nl:publications/e4ca3d42-d7ee-44a9-a80a-4e353a3b066f
      1365318732
    • Contributing Source:
      UNIV OF GRONINGEN
      From OAIster®, provided by the OCLC Cooperative.
    • الرقم المعرف:
      edsoai.on1365318732
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