We have developed a continuous spectrophotometric coupled-enzyme assay for sulfotransferase activity. This assay is based on the regeneration of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) from the desulfated 3'-phosphoadenosine-5'-phosphate (PAP) by a recombinant aryl sulfotransferase using p-nitrophenyl sulfate as the sulfate donor and visible
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
A dietary fiber-deprived gut microbiota degrades the colonic mucus barrier and enhances pathogen susceptibility
Biochemical and biophysical research communications, 271(3), 818-822 (2000-05-18)
The sulfation of a nucleotide is an indispensable step for the sulfuryl group transfer in a biological system. The product and cosubstrate of sulfotransferase in physiological condition are adenosine 3',5'-bisphosphate (PAP) and 3'-phospho adenosine 5'-phosphosulfate (PAPS), respectively. We find that
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
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