Cysteine synthase from rape leaves.

M Masada; K Fukushima; G Tamura

doi:10.1093/oxfordjournals.jbchem.a130811

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PubMed · 1158855

Cysteine synthase from rape leaves.

M Masada·K Fukushima·G Tamura

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Abstract

Cysteine synthase [O-Acetyl-L-serine acetate-lyase (adding hydrogen-sulfide) EC 4.2.99.8] has been highly purified from the extract of rape, Brassica chinensis var. Komatsuna. The purified preparation appeared to be homogeneous on Sephadex G-100 gel filtration and dodecylsulfate-polyacrylamide gel electrophoresis, showing a molecular weight of about 62,000. The latter method also suggested that this enzyme was composed of two identical subunits. The enzyme contained 2 moles of pyridoxal phosphate per mole of enzyme.

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Chromatography, Gel Cysteine Kinetics Lyases Macromolecular Substances Molecular Weight Plants Protein Conformation Pyridoxal Phosphate Serine Subcellular Fractions Journal Article

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M Masada, K Fukushima, G Tamura. 1975. Cysteine synthase from rape leaves.. https://doi.org/10.1093/oxfordjournals.jbchem.a130811

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