RGD Reference Report - Affinity purification and characterization of serine hydroxymethyltransferases from rat liver. - Rat Genome Database

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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.
RGD ID: 2300383
Pubmed: (View Article at PubMed) PMID:3110140

A rapid and simple method was developed for the purification of serine hydroxymethyltransferases [EC 2.1.2.1]. 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.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component
cytosol  (IDA)
mitochondrion  (IDA)

Molecular Function

Molecular Pathway Annotations    
Objects Annotated

Genes (Rattus norvegicus)
Shmt1  (serine hydroxymethyltransferase 1)
Shmt2  (serine hydroxymethyltransferase 2)

Genes (Mus musculus)
Shmt1  (serine hydroxymethyltransferase 1 (soluble))
Shmt2  (serine hydroxymethyltransferase 2 (mitochondrial))

Genes (Homo sapiens)
SHMT1  (serine hydroxymethyltransferase 1)
SHMT2  (serine hydroxymethyltransferase 2)


Additional Information