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- W1796402324 abstract "Publisher Summary This chapter discusses the methods of preparation of Diamine-α-Ketoglutarate Aminotransferase ( Escherichia coli ). One unit of enzyme is defined as the amount of protein which converts 1 micromole of putrescine per minute into γ-aminobutyraldehyde. The specific activity is the units of activity per milligram of protein. The enzyme shows maximum activity between pH 9 and 10. Several amines and amino acids have been tested as substrate with α-ketoglutarate as cosubstrate. Because the method of Hohnstedt does not apply to most of the amines tested, the reactions are followed by isolation and determination of the L -glutamate formed. The enzyme preparation also exhibits transaminase activity toward γ-aminobutyrate. Purified enzyme is normally active without added pyridoxal phosphate. However, an absolute requirement for pyridoxal phosphate is observed when the enzyme is irradiated with ultraviolet light (10 hours) 2 or treated with 2 x 10 -3 M phenylhydrazine and then with Norite. Semicarbazide, hydroxylamine, and cyanide inhibit enzyme activity completely at a concentration of 5 x 10 -4 M." @default.
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- W1796402324 date "1971-01-01" @default.
- W1796402324 modified "2023-09-27" @default.
- W1796402324 title "[252] Diamine-α-ketoglutarate aminotransferase (Escherichia coli)" @default.
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- W1796402324 doi "https://doi.org/10.1016/0076-6879(71)17143-1" @default.
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