The Serine Hydroxymethyltransferase of Plasmodium lophurae*
- 1 May 1976
- journal article
- Published by Wiley in The Journal of Protozoology
- Vol. 23 (2), 282-286
- https://doi.org/10.1111/j.1550-7408.1976.tb03770.x
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.Keywords
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