The serine hydroxymethyltransferase of Plasmodium lophurae
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Updated: Oct 29, 2026
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Generating Genetically Modified Plasmodium berghei Sporozoites
Published on: May 5, 2023
The Journal of Protozoology
|May 1, 1976
Abstract:
Plasmodium lophurae serine hydroxymethyltransferase (EC 2.1.2.1) was partially purified and characterized by (NH4)2SO4 fractionation and chromatography on Sephadex G-100. The enzyme, precipitated by 3.0.3.3 M (NH4)2SO4, had a molecular weight of 68,300 as estimated by exclusion chromatography on G-100. The pH optimum of the enzyme was 6.8-7.6 in sodium phosphate-citrate buffer. Citrate stabilized the enzyme during storage in phosphate buffer at 4 C. The Km was 4.3 X 10(-3) M for L-serine and 2.5 X 10(-4) M for tetrahydrofolate.
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