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- W935910069 abstract "This chapter illustrates the assay, purification, and properties of ornithine aminotransferase. This enzyme occurs widely and is largely purified from Neurospora crassa, rat liver, and pig kidney. Transamination from the amino group of ornithine to α-ketoglutarate proceeds virtually to completion due to the spontaneous cyclization of the product, L-glutamic semialdehyde, to ∆l-pyrroline 5-carboxylate. This latter compound reacts with o-aminobenzaldehyde to form a deep yellow dihydroquinazolium derivative. This enzyme shows restricted substrate specificity. The substrate, α-ketoglutarate, is a powerful inhibitor at low pH values. The enzyme is very sensitive to p-chloromercuribenzoate. This inhibition can be reversed by treatment with mercaptoethanol. With 60 mM L-ornithine and 20 mM α-ketoglutarate, the enzyme is active from pH 7 to 9 with a very sharp optimum at pH 8. The kinetics of this enzyme is complicated by substrate activation and inhibition. α-Ketoglutarate inhibits at low pH values, but ornithine activates at high pH values. The kinetics at high pH values is best described by a binary rate equation at low ornithine concentrations and by a ternary rate equation at higher concentrations." @default.
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- W935910069 date "1970-01-01" @default.
- W935910069 modified "2023-09-23" @default.
- W935910069 title "[31] Ornithine aminotransferase (pig kidney)" @default.
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- W935910069 doi "https://doi.org/10.1016/0076-6879(71)17197-2" @default.
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