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- W2058720711 abstract "Tyrosine hydroxylase from brain homogenates differed from tyrosine hydroxylase from adrenal homogenates in being particle-bound, insensitive to cofactors, possessing a lower Michaelis constant for tyrosine, and being responsive to slightly different optimum conditions of pH and buffer. The combination of 0.02 M mercaptoethanol and 0.1–1.0 mM 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine (DMPH 4 ) increased tyrosine hydroxylase activity in beef adrenal homogenates 15-fold, but was without effect on activity in rat brain homogenates. The K m for tyrosine in beef adrenal homogenates was 4 × 10 −6 M, and in rat brain homogenates was 0.45 × 10 −6 M. Conversion in beef adrenal homogenates was maximum in 0.6 M sodium acetate buffer, pH 6.0, and in rat brain homogenates was maximum in 0.28 M phosphate buffer, pH 6.2." @default.
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- W2058720711 date "1967-10-01" @default.
- W2058720711 modified "2023-09-23" @default.
- W2058720711 title "SOME CHARACTERISTICS OF BRAIN TYROSINE HYDROXYLASE" @default.
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- W2058720711 doi "https://doi.org/10.1139/o67-185" @default.
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