Human platelet thermostable phenol sulfotransferase from blacks and whites: Biochemical properties and variations in thermal stability

Robert J. Anderson, Bertha L. Jackson, Dianne K. Liebentritt

Research output: Contribution to journalArticle

20 Scopus citations


Phenol suifotransferase (PST) catalyzes the sulfate conjugation of catecholamines and of phenolic drugs. Human platelet PST exists in at least a thermolabile form (TL PST) and a thermostable form (TS PST). The mean basal level of platelet TS PST activity in samples from American blacks is significantly higher than the basal activity in samples from whites. We carried out the studies reported here to determine whether the higher basal TS PST activity in platelet homogenates from blacks was biochemically similar to the lower basal activity in samples from whites. We also characterized variations in TS PST thermal stability. Platelet TS PST activities in samples from the two groups were almost identical with respect to pH optima, Michaells-Menten constant values for substrates, and susceptibilities to inhibition by 2,6-dichloro-4-nitrophenol and sodium chloride. Thermolabile and thermostable TS PST were present in samples from both blacks and whites. Thermal stabilities of TS PST in samples from 167 volunteers 104 blacks, 63 whites) were expressed as heated sample-to-control sample ratios. Bimodal frequency distribution histograms of the heated-to-control ratios revealed subgroups of samples with thermolabile TS PST activities from 13.8% of blacks (heated-to-control ratio

Original languageEnglish (US)
Pages (from-to)773-783
Number of pages11
JournalThe Journal of Laboratory and Clinical Medicine
Issue number6
StatePublished - Dec 1988


All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine

Cite this