Zobrazeno 1 - 7
of 7
pro vyhledávání: '"John L. Aull"'
Publikováno v:
Microchemical Journal. 19:210-218
Polyacrylamide gel electrophoresis was used to resolve as many as three protein components from incubation mixtures containing the inhibitor, 5-fluoro-2′-deoxyuridylate, the cofactor, 5,10-methylene tetrahydrofolate, and thymidylate synthetase. In
Publikováno v:
Journal of Biological Chemistry. 251:1303-1310
Ternary complexes of thymidylate synthetase (Form II and Form III), which are composed of the enzyme, 5-fluorodeoxyuridylate, and the natural isomer of methylenetetrahydrofolate, were generated by titrating thymidylate synthetase (Form I) in the pres
Publikováno v:
Archives of Biochemistry and Biophysics. 165:805-808
Publikováno v:
Journal of Biological Chemistry. 249:1167-1172
SUMMARY Carboxypeptidase A treated with diisopropylphosphorofluoridate (DFP) present at catalytic levels causes the complete inactivation of thymidylate synthetase. The rate of this inactivation is shown to be proportional to the concentration of car
Publikováno v:
Journal of Biological Chemistry. 247:566-571
Preparative polyacrylamide gel electrophoresis has been used in the final stages of purification to prepare horse serum cholinesterase which was at least 95% pure, as judged by analytical polyacrylamide gel electrophoresis. The starting material, alr
Publikováno v:
Biochemistry. 16(4)
Thymidylate synthetase (methylenetetrahydrofolate:deoxyuridylate C-methyltransferase) from Lactobacillus casei was progressively inactivated when incubated at 25 degrees C, pH 6.8, in the presence of trans-Pt(NH3)2Cl2. The inhibition appeared to be i
Publikováno v:
Journal of inorganic biochemistry. 22(4)
Thymidylate synthase from methotrexate-resistant Lactobacillus casei rapidly lost about 90% of its catalytic activity when incubated with an equimolar concentration of IO4- at 0 degree C. Nearly complete inhibition resulted when the IO4- concentratio