Purification and Properties of Alanine aminotransferase from Germinating Castor Bean Endosperms

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概要

• 論文の詳細を見る

• Alanine aminotransferase from germinating castor bean endosperms was purified about 1,500-fold by ammonium sulfate fractionation and chromatographies with DEAE-Sepharose CL-6B, TEAE-Cellulose, QAE-Sephadex A-50, and TSK-5PW (HPLC). The molecular weight of the enzyme was about 110kDa, with two identical subunits. The purified enzyme was highly specific for alanine as an amino donor and 2-oxoglutarate as an acceptor, and it showed also glyoxylate transamination activities at low rate. The evidence indicates that alanine: 2-oxoglutarate aminotransferase and glyoxylate aminotransferase activities are associated with the same protein. Pyridoxal phosphate as a cofactor was so tightly bound to the enzyme that added pyridoxal phosphate was not required in the assays. The enzyme showed normal Michaelis-Menten kinetics for all substrates. Reactions proceeded by a Ping Pong Bi Bi mechanism. The K_m for L-alanine, 2-oxoglutarate were 3.4mM and 0.26mM, respectively. The optimum pH was 8.5 and pI was about 4.6.

• 大阪府立大学の論文
• 1995-03-31

著者

• Fujii Michiko

  Laboratory Of Applied Molecular Biology College Of Agriculture

• Yoshii Keiji

  Laboratory Of Applied Molecular Biology College Of Agriculture

関連論文

• Purification and Properties of Fructose-1, 6-Bisphosphatase from Germinating Castor Bean Endosperm
• Purification and Properties of Trehalase from Hemolymph of the Pupae of Blowfly, Aldrichina grahami
• Purification and Properties of Glutamine Synthetase from Germinating Castor Bean Endosperm
• Purification and Properties of Alanine aminotransferase from Germinating Castor Bean Endosperms

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