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  • Title: Purification, relative molecular mass and subunits of thymidylate synthase from Lactobacillus leichmannii.
    Author: Rao KN.
    Journal: Indian J Biochem Biophys; 1993 Feb; 30(1):26-35. PubMed ID: 7685312.
    Abstract:
    Thymidylate synthase (5, 10-methylenetetrahydrofolate: dUMP C-methyltransferase, EC 2.1.1.45) from crude cell extracts of Lactobacillus leichmannii has been purified 190-fold to homogeneity by chromatography on hydroxylapatite, DEAE-cellulose and Sephadex G-100 columns. It has UV absorption maxima at 280 nm. The crude extracts, however, have RNA associated with the native enzyme. This is in line with our earlier observation on the Streptococcus faecium thymidylate synthase [Narasimha Rao K & Kisliuk R L, (1983) Proc Natl Acad Sci USA, 80, 916-920]. Optimal conditions for dTMP synthase activity are: 275 microM (dl)-L-H4PteGlu, 13 mM HCHO, 13 mM MgCl2, 100 microM dUMP and 75 mM 2-mercaptoethanol at pH 7.4 using Tris-HCl buffer. The enzyme has M(r) of 74 kDa, Stokes radius of 1.24 nm and a sedimentation coefficient value of 0.45 S. The enzyme is a dimer composed of 2 identical subunits each with M(r) of 37 kDa.
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