Purification and properties of mouse thymus thymidylate synthase. Comparison of the enzyme from mammalian normal and tumour tissues |
| |
Authors: | W Rode J Cie?la Z Zieliński B Kedzierska |
| |
Affiliation: | Department of Cellular Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur St, 02-093 Warsaw, Poland |
| |
Abstract: | Mouse thymus thymidylate synthase has been purified to apparent electrophoretic homogeneity and compared with the enzyme from mouse tumour L1210 and Ehrlich ascites carcinoma cells. The enzyme is a dimer composed of 35,000 mol. wt monomers. Mouse thymus and tumour enzymes exhibit allosteric properties reflected by cooperative binding of both dUMP and 5-fluoro-dUMP. Activation energy for the reaction, catalyzed by thymidylate synthase from mouse tumour but not from mouse thymus, lowers at temperatures above 34 degrees C, reflecting a change of rate-limiting step in dTMP formation. MgATP at millimolar concentrations inhibits mouse thymus enzyme. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|