Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sodium/copper chlorophyllin (CHL) is a water-soluble derivative of chlorophyll that exhibits antimutagenic activity in several short-term genotoxicity assays and inhibits carcinogen-DNA binding in vivo. The effect of CHL pretreatment on the excretion of mutagens in the urine and feces of male Sprague-Dawley rats has been studied using the Salmonella mutagenicity assay. Animals were given 1 percent CHL in the drinking water for 2 days before administering a single dose of 2-amino-3-methylimidazo-[4,5-f]quinoline (IQ) by oral gavage. Rats pretreated with CHL had higher levels of mutagens in the urine and feces compared with animals given IQ alone; 48 hr after IQ administration, the total mutagenic dose excreted was < 4% in controls vs. 18% in rats given CHL. Mutagenicity required the presence of an activation system, was unaffected by treatment with beta-glucuronidase or arylsulfatase, and in both the urine and feces was accounted for by increased elimination of unmetabolized parent compound. The results support the view that CHL may operate in vivo as a "desmutagen" or interceptor molecule, interacting with IQ in the gut and tissues, and reducing carcinogen bioavailability.
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PMID:Chlorophyllin-enhanced excretion of urinary and fecal mutagens in rats given 2-amino-3-methylimidazo[4,5-f]quinoline. 139 10

Sodium 2-hydroxy-5-nitro-alpha-toluenesulfonate (HNT, compound II, Fig. 7) is a synthetic inhibitor of arylsulfatase (E.C. 3.1.6.1.). At 1 to 10 mM, HNT increased the clotting time of heparinized rabbit blood by 7-fold. In the 6-day chick embryo, mixtures of heparin and hydrocortisone applied to the chorioallantoic membrane, are known to inhibit specifically the growth of capillary blood vessels. HNT potentiated this antiangiogenic activity in a dose-dependent manner when the concentration of heparin was suboptimal. Potentiation of the antiangiogenic activity of steroids by HNT correlated inversely with the concentration of exogenous heparin. In the absence of exogenous heparin, hydrocortisone did not inhibit angiogenesis. Hydrocortisone and HNT, however, inhibited angiogenesis to the same extent as hydrocortisone and heparin. An arylsulfatase with a Km of 1.5 mM for nitrocatechol sulfate as substrate and a Ki of 10.0 microM for the inhibition of HNT, was identified in the chick embryo chorioallantoic membrane. Preincubation of heparin with a commercially available arylsulfatase caused a 50% reduction in antiangiogenic activity of heparin-steroid mixtures applied to the chorioallantoic membrane. This loss of activity was prevented completely by addition of HNT to the arylsulfatase-heparin incubation mixture. These results suggest that HNT (a) potentiates the anticoagulant function of heparin, (b) prevents the inactivation of antiangiogenic activity of heparin by an endogenous arylsulfatase in the chorioallantoic membrane and by a commercial arylsulfatase, and (c) in the presence of angiostatic steroids can inhibit angiogenesis in the chick embryo without the addition of exogenous heparin. On the basis of these data, we propose that this inhibitor of arylsulfatase acts to potentiate angiostatic steroids by suppressing the desulfation of tissue heparin.
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PMID:Potentiation of angiostatic steroids by a synthetic inhibitor of arylsulfatase. 245 97

Pseudomonas C12B grew on and oxidized linear primary alcohols with even- and odd-numbered carbon chains ranging from C(2) to C(11). Cell-free extracts of the bacteria contained a nicotinamide adenine dinucleotide-linked dehydrogenase(s) active with these alcohols and with branched primary and linear secondary alcohols as well. Analysis by gas-liquid chromatography of hexane extracts of filtrates of cultures containing mixtures of even-carbon numbered alcohols from C(10) to C(18) revealed that decanol was rapidly utilized, whereas the remainder were slowly dissimilated up to 19 hr and then were rapidly degraded in the next few hours of culture. The validity for these studies of (i) steam distillation as a method for collecting the alcohols from cultures, and (ii) quantitative estimation by gas-liquid chromatographic comparison with an added internal marker, was established. Steam distillation and gas-liquid chromatography were then used to show that failure to demonstrate stoichiometry of sulfate and dodecanol in the alkyl sulfatase reaction in a previous study resulted from contamination of the commercial "Dodecyl Sodium Sulfate, 95%" used with decyl, undecyl, and tetradecyl sulfates.
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PMID:Metabolism of linear alcohols with various chain lengths by a Pseudomonas species. 595 54

Sodium efflux was studied in 22Na-loaded red blood cells in the presence of arylsulfatase, an enzyme that specifically hydrolyzes sulfatide. Sodium efflux was inhibited in proportion to the amount of arylsulfatase present. Maximum inhibition was almost as high as the efflux obtained in medium with K+ absent. At maximum inhibition 83.2% of the sulfatide content of the fragmented red blood cell membranes was hydrolyzed and ouabain-sensitive (Na+ + K+)-ATPase activity was inhibited by 100%. Sodium efflux, sulfatide content, and (Na+ + K+)-ATPase activity were unaffected with arylsulfatase in the presence of a high concentration of sulfatide. These results indicate that sulfatide plays a specific role in sodium and potassium ion transport. They also suggest that most sulfatide is localized externally in the red blood cell membrane.
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PMID:Sulfatide role in the sodium pump. 627 71