SOME CHARACTERISTICS OF BRAIN TYROSINE HYDROXYLASE

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.