Abstract
Phenol sulphotransferase (E.C. 2.8.2.1, PST) plays an important role in the sulfate conjugation of catecholamines, catecholamine metabolites, and a variety of drugs such as acetaminophen and alpha-methyldopa (Richter, 1940; Axelrod et al., 1959; Levy et al., 1975; Saavedra et al., 1975; Alam et al., 1977). Individual variation in neurotransmitter function and in response to phenolic and catechol drugs might be due, in part, to individual variations in PST activity. Very little is known about the regulation of PST activity in man. One initial step in the study of individual variation in this important enzyme would be to measure PST activity in an easily obtained peripheral tissue. Since blood is the most easily obtained human tissue, the measurement of PST activity in formed blood elements such as erythrocytes and platelets represents one approach to the study of PST activity in man. However, it cannot be assumed that variations in PST activity in blood elements necessarily reflect significant functional variations in sulfate conjugation. It must first be demonstrated that the biochemical characteristics and the regulation of the enzyme in blood are similar to those in other tissues.
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Weinshilboum, R.M., Anderson, R.J. (1981). Phenol Sulphotransferase in Human Platelet and other Tissues: Endogenous Inhibitors, Assay Conditions, Tissue and Substrate Correlations. In: Sandler, M., Usdin, E. (eds) Phenolsulfotransferase in Mental Health Research. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06118-1_2
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DOI: https://doi.org/10.1007/978-1-349-06118-1_2
Publisher Name: Palgrave Macmillan, London
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