International journal of systematic bacteriology, 40(1), 66-70 (1990-01-01)
A rapid (3-h) arylsulfatase assay for cell suspensions of mycobacteria, in which p-nitrophenyl sulfate is used as the substrate, was developed. Arylsulfatase activity was found in cell suspensions of representative strains of Mycobacterium avium, Mycobacterium intracellulare, and Mycobacterium scrofulaceum grown
Drug metabolism and disposition: the biological fate of chemicals, 19(2), 473-477 (1991-03-01)
Although numerous previous reports have characterized the mammalian biotransformation of the organophosphorus insecticides parathion and methyl parathion, questions still remain regarding the toxicological significance of certain metabolic pathways in vivo. The present study utilized rat liver perfusions in order to
Research communications in molecular pathology and pharmacology, 97(2), 131-138 (1997-08-01)
Hepatic uptake of the sulfate conjugate of p-nitrophenol (p-NPsul) has been studied. Uptake clearance of p-NPsul by isolated rat hepatocytes was dependent on p-NPsul concentration, suggesting carrier-mediated transport. The uptake of p-NPsul by isolated rat hepatocytes was inhibited by acetaminophen
Subcellular preparations from rat liver, brain, and kidney and from human liver were tested for their ability to desulfate T3 sulfate (T3SO4). Activity was found associated with the microsomal fraction: rat liver was the most active, hydrolyzing 76 pmol/min.mg protein
The Journal of organic chemistry, 76(22), 9228-9238 (2011-10-11)
Both phosphoryl and sulfuryl transfers are ubiquitous in biology, being involved in a wide range of processes, ranging from cell division to apoptosis. Additionally, it is becoming increasingly clear that enzymes that can catalyze phosphoryl transfer can often cross-catalyze sulfuryl
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