6533b873fe1ef96bd12d4539

RESEARCH PRODUCT

Expression of human estrogen sulfotransferase in Salmonella typhimurium: differences between hHST and hEST in the enantioselective activation of 1-hydroxyethylpyrene to a mutagen.

Ulrike PabelRobert LandsiedelCharles N. FalanyHansruedi GlattIngrid BartschMaria Hagen

subject

Salmonella typhimuriumSalmonellaBlotting WesternMutagenStereoisomerismToxicologymedicine.disease_causeAmes testSubstrate SpecificityCytosolmedicineAnimalsHumansEstrogen SulfotransferaseBenzyl AlcoholsStrain (chemistry)ChemistryMutagenicity Testsfood and beveragesStereoisomerismGeneral MedicineRatsBlotBiochemistryHeterologous expressionSulfotransferasesMutagens

description

Various human sulfotransferases (hP-PST, hM-PST, hHST) and rat sulfotransferases (rPST-IV, rHSTa) have already been expressed in Ames' Salmonella strains (in particular in TA1538). Now a further strain, TA1538-hEST, which expresses the human estrogen sulfotransferase (hEST), has been constructed. This strain activated the primary benzylic alcohol 1-hydroxymethylpyrene (1-HMP) and the secondary benzylic alcohol 1-hydroxyethylpyrene (1-HEP) to mutagens. Human sulfotransferases hEST and hHST both activated 1-HEP, but they differed substantially in their enantioselectivity for this compound.

yearjournalcountryeditionlanguage
1998-05-05Chemico-biological interactions
10.1016/s0009-2797(97)00136-1https://pubmed.ncbi.nlm.nih.gov/9566749