Sa Nga PattanakitsakulAdisorn RatanaphanPintip RuenwongsaMahidol University2018-10-122018-10-121985-01-01Comparative Biochemistry and Physiology -- Part B: Biochemistry and. Vol.80, No.3 (1985), 583-587030504912-s2.0-0021904294https://repository.li.mahidol.ac.th/handle/123456789/307451. 1. Partially purified thymidylate synthetase from Plasmodium berghei and mouse reticulocytes was characterized. 2. 2. The mol. wt of the enzyme from P. berghei was about twice that from mouse reticulocytes. 3. 3. The optimum pH of the enzyme from P. berghei was found to be 6.5-7.5 while that from the host was 7.0-8.0. 4. 4. The enzyme from P. berghei was more susceptible to pH denaturation than the enzyme from reticulocytes. 5. 5. The enzyme from both sources differed in their Kmvalues for substrates. 6. 6. The enzyme from reticulocytes was less sensitive to inhibition by substrate analogs than that from P. berghei. © 1985.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1016/0305-0491(85)90295-0