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In 3 patients with proved pheochromocytoma, circulating catecholamine concentrations, vanillylmandelic acid and total free catecholamine urinary excretion, dopamine-beta-hydroxylase activities in plasma were measured the day before surgery, during the removal of the tumour and postoperatively. Following the removal of the pheochromocytoma, all these parameters declined with a different rate, possibly related to the half-life proper to each molecule. The results showing a decrease in plasma D beta H activities after the removal of the tumors are in good accordance with most authors. The mechanism and the meaning of catecholamines release from non-innervated tumor-cells remain to be elucidated. By considering these three cases, it does not seem that the evolution of D beta H activity after removal of the tumor is dependent upon the fact that the pheochromocytoma releases preferentially either epinephrine or nephinephrine.

L-DOPA decarboxylase was purified from rat pheochromocytoma. Tryptic digestion of this enzyme permitted obtaining fourteen peptides. The comparison of the sequence of L-DOPA decarboxylase from other species with one of these peptides demonstrates a great preservation of this protein.

Rat pheochromocytoma contains a protein kinase activity which remains associated with tyrosine hydroxylase (TH) during its purification. The incorporation of phosphate in TH is observed after incubation of TH with labelled ATP and magnesium without the need for an exogenous protein kinase. This Ca2+ and cAMP-independent kinase activity is different from previously described TH phosphorylating kinases from rat pheochromocytoma and other tissues.