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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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