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The Serine Hydroxymethyltransferase of Plasmodium lophurae (1976)

PLATZER, EDWARD G. ; CAMPUZANO, HELEN C.

Oxford, UK : Blackwell Publishing Ltd

The @journal of eukaryotic microbiology 23 (1976), S. 0

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ISSN: 1550-7408

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: SYNOPSIS. 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 × 10−3m for l-serine and 2.5 × 10−4m for tetrahydrofolate.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1550-7408.1976.tb03770.x

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