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• W1998364360 abstract "Tryptophan hydroxylase (EC 1.14.16.4; L-tryptophan, tetrahydropteridine: oxygen oxidoreductase (5-hydroxylating)) from rat mesencephalic tegmentum has been purified by sequential chromatography on Blue-Sepharose, DE-52, and calmodulin-Sepharose. The hydroxylase is excluded from Blue-Sepharose and is eluted from DE-52 with a step-wise NaCl gradient. Tryptophan hydroxylase binds to calmodulin-Sepharose in the presence of calcium and is eluted with either EGTA or calmodulin itself, but not with tryptophan. The purification scheme is rapid (5-6 h) and yields an enzyme with a specific activity of 225 nmol 5-HTP/mg min, representing a 400-fold purification with 7% recovery. The tryptophan hydroxylase preparation was judged to be > 95% pure using the present isolation procedure." @default.
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• W1998364360 date "1996-11-01" @default.
• W1998364360 modified "2023-09-24" @default.
• W1998364360 title "Tryptophan hydroxylase: Purification by affinity chromatography on calmodulin-Sepharose" @default.
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• W1998364360 doi "https://doi.org/10.1016/s0165-0270(96)00034-9" @default.
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