Abstract
Thymidylate synthetase in mouse erythrocytes infected with Plasmodium berghei increases markedly during cellular parasitization. The malaria enzyme has been compared with enzymes from normal mouse reticulocytes and Escherichia coli by kinetic and physical means. When folic acid analogues were used as cofactors, distinct kinetic differences were apparent when thymidylate synthetases from P. berghei and E. coli were compared. However, no significant kinetic dissimilarities were revealed in a comparison of enzymes from P. berghei and the host mouse reticulocytes. Upon gel filtration the P. berghei thymidylate synthetase exhibits an apparent molecular weight in excess of 100,000 whereas the normal mouse reticulocyte enzyme shows an apparent molecular weight of 68,000, similar to the enzyme from E. coli.
- Copyright ©, 1973, by Academic Press, Inc.
MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|