Purification and Properties of Glutamate Synthase from Germinating Castor Bean Cotyledons

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概要

• 論文の詳細を見る

• The activity of glutamate synthase in germinating castor bean cotyledon was found to increase rapidly from the 3rd to 4th day of germination. The enzyme was purified about 220-fold by ammonium sulfate fractionation and chromatographies with DEAE-Sephadex, Sephadex G-200, Affi-Gel Blue and Sephadex G-150. The purified enzyme can accept electrons from NADH for the enzyme reaction, but it cannot use NADPH. The enzyme has a molecular weight of 76,000. The optimum pH was 8.5. The enzyme showed normal Michaelis-Menten kinetics for all substrates. Apparent K_m values for L-glutamine, 2-oxoglutarate and NADH were 30mM, 330μM and 8μM respectively. The enzyme activities were inhibited by L-glutamate, ATP, GTP, pyrophsphate, citrate and isocitrate. Only phosphate and aspartate enhanced the enzyme activity. Sulfhydryl reagents was strong inhibitor.

• 大阪府立大学の論文
• 1994-03-31

著者

• Fujii M

  Univ. Osaka Prefecture Osaka Jpn

• YOKAWA Kenichi

  Laboratory of Biochemistry, College of Agriculture

• Yokawa Kenichi

  Laboratory Of Biochemistry College Of Agriculture

関連論文

• Purification and Properties of Glutamate Synthase from Germinating Castor Bean Cotyledons

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