Human pheochromocytoma phenol sulfotransferase: biochemical properties and activities of thermolabile and thermostable forms.

To determine whether pheochromocytoma phenol sulfotransferase (PST) activities were similar to blood platelet PST activities, we established assay conditions and biochemical properties for the human pheochromocytoma enzymes. At least two forms of PST were present in high speed supernatant (HSS) preparations of the tumors. A thermolabile form (TL) and a thermostable form (TS) were similar to those of human platelet PST with regard to pH optima, apparent Km values, responses to 2,6-dichloro-4-nitrophenol and thermal stability. PST activities were measured in 74 tumors of neuroectodermal origin that had been stored at -80 degrees C for a mean of 37.9 months. Levels of TL and TS PST activities decreased in a nonlinear fashion with time of sample storage. TL and TS PST activities of 4 samples assayed after 1.08 +/- 1.95 (mean +/- SD) month of storage were 167 +/- 73 and 3,110 +/- 1,817 U/mg protein, respectively (mean +/- SEM). Our results indicated that the TL and TS forms of PST in pheochromocytoma HSS preparations were biochemically similar to platelet PST activities.

Human pituitary phenol sulfotransferase: biochemical properties and activities of the thermostable and thermolabile forms.

Pituitary tissue contains phenol sulfotransferase (PST), the enzyme that catalyzes the sulfate conjugation of monoamine neurotransmitters. We carried out these studies with pituitaries obtained 21.3 +/- 3.0 h postmortem (mean +/- SEM; n = 21) to determine whether the biochemical properties and variations in levels of human pituitary PST activities were similar to those of PST in platelets from control subjects. PST in the human platelet has been studied thoroughly because of the possibility that platelet PST might reflect levels of PST activity in other tissues such as the pituitary and brain. Our results demonstrated 2 forms of the pituitary enzyme that were similar to the thermostable (TS) and thermolabile (TL) forms of platelet PST with regard to assay conditions, pH optima, Km values for multiple substrates, responses to 2,6-dichloro-4-nitrophenol (DCNP), and thermal stability properties. Pituitary samples also were obtained at autopsy 6.3 +/- 0.33 h (mean +/- SEM; n = 3) after death to determine the effects of storage at 4 degrees C on PST activities. After storage for 6-18 h, 83-99.6% of the TS PST activity remained and 44-66.9% of the TL PST activity remained. Pituitary TS PST activity in samples obtained within 12.1 +/- 3.25 h after death was 121.0 +/- 49.1 units/mg protein (mean +/- SEM; n = 7) with a range from 9.7 to 367.6. TL PST activity was 35.6 +/- 11.6 units/mg protein (mean +/- SEM; n = 6) with a range from 6.1 to 80.7. Wide variations of both enzyme activities were also present in 3 pituitary tumor samples.(ABSTRACT TRUNCATED AT 250 WORDS)