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|Title:||An HPLC-ECD procedure for measuring total phenolsulfotransferase (PST) activity in human liver, platelets and blood|
|Citation:||Khoo, B.Y., Sit, K.H., Wong, K.P. (1990). An HPLC-ECD procedure for measuring total phenolsulfotransferase (PST) activity in human liver, platelets and blood. Clinica Chimica Acta 194 (2-3) : 219-228. ScholarBank@NUS Repository. https://doi.org/10.1016/0009-8981(90)90136-G|
|Abstract:||The phenolsulfotransferase (PST) activity in human liver, platelets and blood was measured under saturating concentrations of the conjugating agent, 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Conventional PST assays employ PAP35S at suboptimal concentrations. In addition, the sulfate conjugate formed, namely N-acetyldopamine-sulfate (NADA-sulfate) was quantified directly by high-pressure liquid chromatography cum electrochemical detection (HPLC-ECD). NADA, the biogenic amine acceptor used in this study appeared from kinetic data to be a substrate of both the P and M forms of PST when used in micromolar concentration. Two apparent K(m) values of 4.2 μmol/l and 22.6 μmol/l were observed. In contrast, only one apparent K(m) value was evident when the assay was carried out in the presence of 2,6-dichloro-4-nitrophenol (DCNP), a selective inhibitor of the P form of PST or after heat treatment under specified conditions which inactivates the M form of PST. Thus measurement of PST activity with NADA as the acceptor substrate permits the determination of total PST activity and a parallel assay with the inclusion of DCNP would distinguish the two variants of PST, both of which appear to be present in all human tissues.|
|Source Title:||Clinica Chimica Acta|
|Appears in Collections:||Staff Publications|
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