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

A new method is described for the direct cytochemical demonstration of lysosomal arylsulfatases utilizing a synthetic substrate, 4-nitro-1,2-benzenediol mono(hydrogen sulfate), and a copper capture reaction. A small amount of Hatchett's brown (cupric ferrocyanide, Cu2Fe(CN)6-7 H2O) formed at the subcellular sites of copper capture is then utilized as a heterogeneous catalyst to effect the oxidative polymerization of 3,3'-diaminobenzidine which results in the formation of an insoluble, highly colored osmiophilic indamine polymer at the sites of enzymatic activity. The reaction product even at this stage prior to osmication is highly visible. It is readily seen with a light microscope in 50 mum sections of fixed tissues prepared with a mechanical chopper or in 10 micron cryostat sections treated for arylsulfatase activity. Upon osmication, an electron-opaque osmium black is formed which is much less soluble than the products of either the lead or barium capture reactions currently used for the demonstration of arylsulfatase with the electron microscope. The selection of areas of plastic-embedded tissues for ultrathin sectioning is facilitated by the ready visibility of these osmium black end products on 1-2 mum plastic sections which can be studied with the light microscope. This method gives permanent specimens demonstrating arylsulfatases A or B in lysosomes and autophagic vacuoles. In addition, enzyme activity is seen occasionally in the Golgi region or lamellae of certain cells believed to be elaborating sulfated products. In these instances, it may be demonstrating sulfotransferase activity.
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PMID:The demonstration of arylsulfatases with 4-nitro-1,2-benzenediol mono(hydrogen sulfate) by the formation of osmium blacks at the sites of copper capture. 4 59

Mucopolysaccharidoses (MPS) are a group of inherited lysosomal storage disorders, each with deficiency of an enzyme degrading glycosaminoglycans (GAG). To increase the ability to differentiate each of the disorders, the N-acetyl-galactosamine-4-sulfatase (arylsulfatase B) activity was measured in human peripheral leukocytes and skin fibroblasts. The assay employed p-nitrocatechol sulfate as an artificial substrate, and barium salt as an inhibitor to arylsulfatase A. Applying this method, a case of Maroteaux-Lamy syndrome (MPS type VI) was recognized in a six-year-old girl who had cloudy cornea, coarse-appearing face, mucopolysacchariduria, and white cell metachromasia. Her body height and mentality were normal. Arylsulfatase B activity in her skin fibroblasts was around 5% of normal. Diagnosis of MPS VI, especially in its milder form, depends on enzyme test.
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PMID:Quantification of arylsulfatase B activity and diagnosis of Maroteaux-Lamy syndrome. 177 56

Kurloff cells are mononuclear cells characterized by a large metachromatic and PAS-positive inclusion called the Kurloff body. Bone-marrow and spleen Kurloff cells were incubated with p-nitrocatechol sulfate as substrate and barium chloride as capturing agent for the ultracytochemical detection of the lysosomal marker enzyme, arylsulfatase. Enzymatic reaction product was consistently found as a single spot-like deposit confined to the rim of the Kurloff body. These results, and the previously described presence of other acid hydrolases and sulfated glycosamino++glycans, emphasize the similarities between the Kurloff body and lysosomes. Reaction product could also be found occasionally in segments of the rough endoplasmic reticulum but it was absent from the Golgi apparatus. This arylsulfatase activity could be related to the natural killer activity of Kurloff cells.
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PMID:Cytochemical localization of arylsulfatase in guinea-pig Kurloff cells. 314 42

Metal precipitation techniques for ultrastructural demonstration of arylsulfatase C activity were studied in rat kidney. Possible substrates for the techniques were biochemically tested with regard to their velocity of enzymatic hydrolysis and their specificity for arylsulfatase C. Effects of buffers and capturing metals were also examined. The results of these biochemical studies were then verified histochemically. Incubation in a medium containing 1 mM 4-methylumbelliferyl sulfate, 1% barium chloride, 0.1 M imidazole-HCl buffer (pH 7.5), and 5% sucrose achieved identifiable results in adequately fixed kidney. Precipitation of barium sulfate was localized mainly in the endoplasmic reticulum and perinuclear cisterns of the epithelial cells in the descending portions of proximal tubules.
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PMID:Ultrastructural localization of arylsulfatase C activity in rat kidney. 347 Mar 83

Alkyl sulfatase was induced by growth on nutrient broth plus sodium dodecyl sulfate (SDS) in a bacterium we have designated Pseudomonas C12B. Measurement of the radioactivity of S(35)O(4) (=) released from SDS(35) by the enzyme in cell-free extracts provided an effective assay technique. The barium chloranilate assay for release of SO(4) (=) from SDS was somewhat less sensitive but effective if analyzed at 332 mmu. This test was only approximately 55% as sensitive if analyzed at 530 mmu. The activity of the glyoxylate bypass enzymes, isocitrate lyase and malate synthetase, was significantly stimulated by growth of the bacteria on SDS as the sole carbon source, but not by growth on nutrient broth or nutrient broth plus SDS.
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PMID:ENZYMES INDUCED IN A BACTERIUM BY GROWTH ON SODIUM DODECYL SULFATE. 1420 Oct 90