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Affinity purification and characterization of serine hydroxymethyltransferases from rat liver.

Authors: Masuda, T  Sakamoto, M  Nishizaki, I  Hayashi, H  Yamamoto, M  Wada, H 
Citation: Masuda T, etal., J Biochem. 1987 Mar;101(3):643-52.
Pubmed: (View Article at PubMed) PMID:3110140

A rapid and simple method was developed for the purification of serine hydroxymethyltransferases [EC]. The procedure involved ammonium sulfate precipitation, DEAE-cellulose column chromatography and affinity chromatography on an L-adsorbent. Through this procedure the cytosolic enzyme (s-SHMT) was purified 1,650-fold, and the mitochondrial enzyme (m-SHMT) 1,730-fold, with a yield of more than 30% in both cases. Both preparations gave a single band with a Mr of 54,000 on SDS-PAGE. The native enzymes both contained 4 mol of pyridoxal phosphate/mol of enzyme, and showed a Mr value of 220,000 on gel filtration, indicating a tetrameric structure. Several other properties of the enzymes were also studied.


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CRRD Object Information
CRRD ID: 2300383
Created: 2008-09-16
Species: All species
Last Modified: 2008-09-16
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.