Effect of runway training on rat brain tyrosine hydroxylase: Differential effect of continuous and partial reinforcement schedules

1979 ◽  
Vol 15 (2-3) ◽  
pp. 211-215 ◽  
Author(s):  
M.R. Boarder ◽  
J. Feldon ◽  
J.A. Gray ◽  
Marianne Fillenz
Keyword(s):  
Tyrosine Hydroxylase ◽  
Rat Brain ◽  
Differential Effect ◽  
Partial Reinforcement ◽  
Reinforcement Schedules ◽  
Runway Training ◽  
Brain Tyrosine Hydroxylase

SOME CHARACTERISTICS OF BRAIN TYROSINE HYDROXYLASE

1967 ◽  
Vol 45 (10) ◽  
pp. 1557-1563 ◽  
Author(s):  
E. G. McGeer ◽  
S. Gibson ◽  
P. L. McGeer
Keyword(s):  
Tyrosine Hydroxylase ◽  
Rat Brain ◽  
Phosphate Buffer ◽  
Sodium Acetate ◽  
Acetate Buffer ◽  
Sodium Acetate Buffer ◽  
Optimum Conditions ◽  
Hydroxylase Activity ◽  
Michaelis Constant ◽  
Brain Tyrosine Hydroxylase

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 (DMPH4) increased tyrosine hydroxylase activity in beef adrenal homogenates 15-fold, but was without effect on activity in rat brain homogenates. The Km 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.

Synthesis of [3′,5′-3H2]-α-fluoromethyl-tyrosine as a radioactive specific label of rat brain tyrosine hydroxylase

1994 ◽  
Vol 2 (8) ◽  
pp. 827-835 ◽  
Author(s):  
Pierre Lafargue ◽  
Alain Dodi ◽  
Michel Ponchant ◽  
Christine Garcia ◽  
Marion Le Cavorsin ◽  
...  
Keyword(s):  
Tyrosine Hydroxylase ◽  
Rat Brain ◽  
Specific Label ◽  
Brain Tyrosine Hydroxylase

IN VITRO SCREEN OF INHIBITORS OF RAT BRAIN TYROSINE HYDROXYLASE

1967 ◽  
Vol 45 (1) ◽  
pp. 115-131 ◽  
Author(s):  
E. G. McGeer ◽  
P. L. McGeer
Keyword(s):  
Tyrosine Hydroxylase ◽  
Rat Brain ◽  
Inhibitory Activity ◽  
Brain Homogenate ◽  
Inhibitory Effect ◽  
Side Chain ◽  
Complexing Agents ◽  
Hydroxy Groups ◽  
Brain Tyrosine Hydroxylase

Over 600 compounds were tested at 10−4 M concentration as inhibitors of tyrosine hydroxylase activity in crude rat-brain homogenate. Most of the compounds had little or no inhibitory effect and those with strong inhibitory properties were, except for a very few oxidizing and complexing agents, all close structural analogues of tyrosine or of its catechol metabolites. Data obtained in this screen are generally in accord with previous data reported in the literature. For high inhibitory activity in the tyrosine series, side-chain substitution is critical. N-Substitution is particularly undesirable. For high inhibitory activity in the catechol series, the ring hydroxy groups should be 3,4 in relation to a C—C—N side chain. Further ring substitution is undesirable, but some side-chain substitution is permissible.

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