Isolation of Serine Acetyltransferase Complexed with Cysteine Synthase from Allium tuberosum(Biological Chemistry)
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概要
- 論文の詳細を見る
Serine acetyltransferase (SATase, EC 2.3.1.30), an enzyme which catalyzes the biosynthesis of O-acetyl-L-serine(OAS) from L-serine and acetyl-CoA, has been purified about 33,000-fold with a yield of 11% from leaf extracts of Allium tuberosum with a procedure involving heat treatment, ammonium sulfate fractionation, DEAE-Toyopearl chromatography, Ultrogel AcA34 gel filtration, and Blue-Toyopearl affinity chromatography, followed by a second filtration through Ultrogel AcA34. The isolated enzyme was apparently homogeneous as shown by PAGE with a specific activity of 231 units/mg protein. Besides this SATase activity the enzyme also had a significant level of cysteine synthase(CSase, EC 4.2.99.8)activity with a specific activity of 39.2 units/mg protein. The molecular weight of the enzyme was 650,000 by gel filtration. Subunit analysis by SDS-PAGE yielded two kinds of protein bands with a large subunit molecular weight of 35,000 and a small subunit molecular weight of 31,000. The results of Western blotting analysis using anti-rape CSase IgG suggested that the large subunit could be the CSase subunit.
- 社団法人日本農芸化学会の論文
- 1990-03-23
著者
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TAMURA Goro
Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University
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Tamura Goro
Department Of Agricultural Chemistry Faclty Of Horticulture Chiba University
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Nakamura Katsuhito
Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University
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Nakamura Katsuhito
Department Of Agricultural Chemistry Faculty Of Horticulture Chiba University
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