A monospecific antibody against tyrosine hydroxylase (TH), purified from a transplantable rat
pheochromocytoma, was produced in rabbits. Immunohistochemical techniques were …

We sought to develop a quantitative immunocytochemical procedure using the peroxidase-
antiperoxidase (PAP) technique to analyze amounts of the neurotransmitter biosynthetic …

AN IMMWOCWMICALSTUDYOFTHE INDUCTION OFTYR0SINEHYDROXYLASE
INRATADRENAL R. Hoeldtke, T. Lloyd, andS. Kaufman National Institute o Page 1 Vol. 57, No. 4 …

The enzyme, tyrosine hydroxylase (TH, EC 1.14. 16.3) catalyzes the rate limiting step in the
biosynthesis of catecholaminesL Because of difficulties in isolating the enzyme, the …

The enzyme tyrosine hydroxylase (TH) was immunohistochemically localized by the
peroxidase-antiperoxidase method in rat to chromaffin cells of the adrenal medulla, large …

Approximately 90% of the total tyrosine hydroxylase activity of bovine adrenal medulla
homogenates was localized in the particulate fraction of the homogenate. The particulate …

The enzyme tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of
catecholamines in dopaminergic and noradrenergic neurons of the brain, in sympathetic …

Tyrosine hydroxylase (TH) was isolated from human brain (caudate nucleus+ putamen). The
major form of the active enzyme in the cytoplasmic fraction was purified to apparent …

By using an antibody to human tyrosine hydroxylase (TH) in conjunction with the peroxidase-
anti-peroxidase (PAP) technique 12 we have found it possible to map catecholaminergic …

Tyrosine hydroxylase (TH) was purified from the soluble fraction of human adrenal glands.
The enzyme in human adrenal glands that was purified to apparent homogeneity had an …