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- W2043287750 abstract "1. After preliminary purification of the brain transaminases by acetone precipitation, they were separated by chromatography on a calcium phosphate column, and eluted with phosphate buffers of increasing molarity. The enzymes were further purified by gel filtration on Sephadex G-200. A 100-fold purification of transaminase II and a 25-fold purification of transaminase III were regularly obtained. 2. Transaminase II showed its highest activity towards tyrosine and phenylalanine, while the indole amino acids also were transaminated to a certain degree by this enzyme. 3. Transaminase III showed its highest activity towards tryptophan and 5-hydroxytryptophan while the phenyl amino acids also were transaminated to a certain degree by this enzyme. 4. α-Oxoglutaric and oxaloacetic acids were active as amino acceptors, and in high concentrations they inhibited the transaminases. 5. The optimum pH's were 8.2 and 8.1, respectively." @default.
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- W2043287750 date "1965-01-01" @default.
- W2043287750 modified "2023-10-09" @default.
- W2043287750 title "Separation and purification of aromatic amino acid transaminases from rat brain" @default.
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- W2043287750 doi "https://doi.org/10.1016/0005-2787(65)90612-x" @default.
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