The Interaction of Pteroylpolyglutamates with Calf Thymus Thymidylate Synthase

  • Chandra M. Dwivedi
  • Roy L. Kisliuk
  • Charles M. Baugh
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 163)


Calf thymus thymidylate synthase was purified to homogeneity using a pteroyltetraglutamyllysine Sepharose affinity column. Inhibition of the purified enzyme by folate or methotrexate was enhanced by addition of γ-Glu residues. Tetrahydrofolate, tetrahydropteroyltriglutamate and tetrahydropteroylheptaglutamate, all having the natural configuration at C-6, all showed similar Km values near 15 μM. Thus, although calf thymus thymidylate synthase showed a higher affinity for pteroylpolyglutamates than pteroylmonoglutamate, this was not reflected in lowered Km values with the corresponding tetrahydropteroylpolyglutamate substrates.


Potassium Phosphate Solid Phase Peptide Synthesis Pure Enzyme Thymus Gland Natural Configuration 
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Copyright information

© Springer Science+Business Media New York 1983

Authors and Affiliations

  • Chandra M. Dwivedi
    • 1
  • Roy L. Kisliuk
    • 1
  • Charles M. Baugh
    • 2
  1. 1.Department of Biochemistry and PharmacologyTufts University School of MedicineBostonUSA
  2. 2.Department of BiochemistryUniversity of South Alabama College of MedicineMobileUSA

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