Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Twenty morphologically similar strains of a Mycobacterium sp isolated from milk of cows with bovine mastitis in the US Department of Agriculture dairy herd were identified as M smegmatis. Mastitis isolates submitted from Vermont and Washington also were identified as M smegmatis. A scheme for presumptive identification of rapidly growing mycobacteria was developed, using culture media and bacteriologic techniques commonly used in mastitis diagnostic laboratories. Important tests used were acid-fast staining, rapidity of growth, pigmentation, nitrate reduction, arylsulfatase activity, mucic acid utilization, acid production from galactose, rhamnose, and inositol, and growth at 45 C and 52 C.
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PMID:Characterization and identification of Mycobacterium smegmatis in bovine mastitis. 359 73

The biosynthesis of lysosomal acid phosphatase was studied in a normal human embryonic lung cell line, WI-38. Cells were labeled with radioactive leucine under a variety of conditions, the enzyme was immunoprecipitated using a monospecific antiserum raised against human liver lysosomal acid phosphatase, and the products were separated by electrophoresis and were visualized by fluorography. Lysosomal acid phosphatase constitutes 60% of the total tartrate-inhibitable acid phosphatase in WI-38. It is initially synthesized as a high-molecular-weight precursor polypeptide of 69 kDa. The precursor polypeptide is rapidly glycosylated and processed to a mature enzyme of 53-45 kDa via intermediates of 65 and 60 kDa in WI-38 cells. The 69-kDa precursor polypeptide is also converted to larger precursor polypeptides of 74 and 80 kDa. The multiplicity of precursor polypeptides is due at least in part to differences in the glycosylation and phosphorylation of the polypeptides. Sensitivity of phosphorylated oligosaccharide chains from precursor, mature and small polypeptides to endo-beta-hexosaminidase H-catalyzed cleavage suggests the presence of high-mannose phosphorylated oligosaccharide chains similar to those present on many other lysosomal enzymes. The effects of tunicamycin and ammonium chloride were also studied. In contrast to the effect of ammonium chloride on arylsulfatase A secretion, the lysosomal acid phosphatase in WI-38 cells was not secreted in the presence of NH4Cl. This is consistent with the existence of an alternate route for the transfer of lysosomal acid phosphatase into lysosomes. This alternate route may be the reason that I-cell fibroblasts contain a normal level of lysosomal acid phosphatase.
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PMID:Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells. 390 32

Previous cytochemical and biochemical studies have shown an increase in the activity of acid phosphatase and arylsulfatase during the induction of galactose cataracts in rat lenses. It was postulated that these enzymes may be involved in lens fiber degradation observed during cataractogenesis, however, the role of these enzymes in the repair process was not ruled out. The present investigation has evaluated the level of acid phosphatase activity in lenses in which the induction of opacity is inhibited with the aldose reductase inhibitor sorbinil and during the recovery of galactose induced opacity. Sprague-Dawley rats received 50% galactose diet, or galactose diet with sorbinil, or laboratory chow diet. Following 20 days on this diet all rats received lab chow plus 50 mg kg-1 sorbinil (recovery diet). The lenses were removed at desired intervals following the initiation of the above three diets and following the transfer of animals to the recovery diet. Cytochemical localization and biochemical quantitation of acid phosphatase activity were performed with methods previously reported. Most of the enzyme activity was localized within the epithelial cells and superficial cortical fibers. In the epithelial cell layer, the enzyme activity was primarily localized in lysosomes and at extracellular sites near the epithelial cell membrane which abut each other and cortical fibers. In cortical fibers the enzyme activity was observed at various extracellular sites between the cell membranes of neighboring fibers. The effect of sorbinil, if any, and the possible role of acid hydrolases in the repair process during cataract reversal is discussed.
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PMID:Acid phosphatase II. Cytochemical localization in lenses of normal and galactose-fed rats. 392 63

More than twenty different enzyme activities of fractions containing dictyosome-like structures (DLS) as a dominant cell component were monitored. Plasma membrane vesicles were a major contaminant of the DLS fractions, which, presumably as a consequence, were enriched somewhat in plasma membrane markers. The lysosomal enzymes arylsulfatase and latent acid phosphatase were present in the DLS fractions as were the Golgi apparatus activities thiamine pyrophosphatase and nucleoside diphosphatase. The presence of the latter two enzymes in DLS, plus NADH-ferricyanide reductase, has been verified from cytochemistry. On the other hand, the Golgi apparatus marker, galactosyltransferase, was not enriched in DLS fractions and appeared to be absent. This latter finding, verified from cytochemistry with isolated DLS fractions and, in situ, from [3H]galactose incorporation by testis tubules with analysis by autoradiography, provides the first clear biochemical characteristic that serves unequivocally to distinguish DLS from conventional Golgi apparatus.
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PMID:Dictyosome-like structures from guinea-pig testes lack galactosyltransferase, a Golgi apparatus marker. 392 20

We have demonstrated an increase in activity of arylsulfatase A and B during galactose induced cataract development in rats. Our recent investigation shows that acid phosphatase activity, which increases substantially during galactose cataract development in rats, could be contained to near normal level if Sorbinil, an aldose reductase inhibitor, was fed along with galactose to the rat. We have observed that the activity of other lysosomal enzymes, arylsulfatase A and/or B, also increases during galactose cataractogenesis. In the present report, we provide information with regards to the effect of Sorbinil on the activity of these enzymes during cataractogenesis. A modified Hopsu-Havu and Helminen method (1974) with p-nitrocatecholsulfate as substrate was used for localization of both arylsulfatase A and B; and the method of Hara et al. (1979) was utilized to obtain quantitative data on the level of arylsulfatase A and B activity. Ultrastructural cytochemistry shows that arylsulfatase activity in all lenses was primarily localized in epithelial cells in lysosomes with very little or no activity in cortical fibers. The number of arylsulfatase positive lysosomes and the activity level of these enzymes increased with the progression of cataract development. Galactose induced damage to lens morphology and increase in activity of arylsulfatase A and B was inhibited by inclusion of 50mg/Kg (diet) Sorbinil in the galactose containing cataractogenic diet. However, Sorbinil had no significant effect on the enzyme activity following the establishment of mature cataracts.
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PMID:Ultrastructural cytochemistry: effect of Sorbinil on arylsulfatases in cataractous lenses. 402 88

Rabbit liver aryl sulfatase A (aryl-sulfate sulfohydrolase, EC 3.1.6.1) is a glycoprotein containing 4.6% carbohydrate in the form of 25 residues of mannose, seven residues of N-acetylglucosamine, and three residues of sialic acid per enzyme monomer of molecular weight 140 000. Each monomer consists of two equivalent polypeptide chains. The protein has a relatively high content of proline, glycine and leucine, and the amino acid composition of rabbit liver aryl sulfatase A is similar to that of other known liver sulfatases. Rabbit liver aryl sulfatase A catalyzes the hydrolysis of a wide variety of sulfate esters, although it appears possible that cerebroside sulfate is a physiological substrate for the enzyme because the Km is very low (0.06 mM). The turnover rate for hydrolysis of nitrocatechol sulfate or related synthetic substrates is much higher than the rate with most naturally occurring sulfate esters such as cereroside sulfate, steroid sulfates, L-tyrosine sulfate or glucose 6-sulfate. However, the turnover rate with ascorbate 2-sulfate is comparable to the rates measured using most synthetic substrates. These results are discussed in relationship to several previously described sulfatase enzymes which were claimed to have unique specificities.
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PMID:Chemical characterization and substrate specificity of rabbit liver aryl sulfatase A. 610 85

The brain-specific arylsulfatase Bm (aryl-sulfate sulfohydrolase, EC 3.1.6.1) was demonstrable in human and monkey brain. Arylsulfatases A, B and Bm were separated employing DEAE-cellulose chromatography. There was a distinct difference in the proportion of the sulfatases in infant and adult human brain. Arylsulfatase Bm after concanavalin A-Sepharose chromatography showed the property of binding to Sephadex G-200 totally. Several dissociating agents failed to elute the enzyme from the bound form. Under similar conditions arylsulfatase A did not show any binding to Sephadex. On treatment with Escherichia coli alkaline phosphatase adult human brain arylsulfatase Bm but not arylsulfatase A was converted into a less acidic, presumably dephosphorylated form that did not bind to DEAE-cellulose. Monkey brain arylsulfatase Bm showed a similar susceptibility to E. coli phosphatase treatment. Inorganic phosphate and serine phosphate but not mannose 6-phosphate could inhibit this dephosphorylation. There were differences in the susceptibilities to alkaline phosphatase treatment of the arylsulfatase Bm from infant and adult human brain. Endogenous phosphatase also seemed to have a role on the phosphorylated state of arylsulfatase Bm.
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PMID:Soluble arylsulfatases of human brain and some characteristics of the brain-specific arylsulfatase Bm. 610 86

Trembler mice are affected by dominantly inherited neuropathy. Total lipid content and sulfatides were decreased in peripheral nerves from 15-day-old mutants. The proportion of sulfatides in per cent of total lipids was similar in control and Trembler nerves. The specific activity of ceramide galactosyltrnsferase, the enzyme responsible for the synthesis of cerebrosides, was 36 and 13% of controls, in young and adult. Trembler nerves, respectively. In contrast, cerebroside sulfotransferase activities were increased by 257 and 172% in young and adult Trembler sciatic nerves, respectively. No activator or inhibitor effect could be demonstrated. In Trembler PNS, Km, Vmax and heat sensitivity of CST differed from controls. Low levels of substrate and high arylsulfatase A activity (218% of controls) could explain the lack of sulfatide accumulation. The increased in vivo sulfate and galactose incorporation into non-lipidic material couild reflect the overproduction of endoneurial and perineurial connective tissue, whereas the high turnover rate of sulfatides could be correlated with intense demyelination and remyelination observed in Trembler PNS.
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PMID:Abnormal sulfate metabolism in a hereditary demyelinating neuropathy. 610 27

Biosynthesis of arylsulfatase A in normal and mutant human fibroblasts was studied by growing cells in the presence of L-[4,5-3H] leucine or [2-3H] mannose, isolation of labelled arylsulfatase A by immune precipitation and visualization of electrophoretically separated polypeptide by fluorography. Arylsulfatase A was synthesized as a precursor with a mean apparent molecular mass of 62 kDa. Intracellularly the precursor was converted into a 60.5 kDa polypeptide within a chase period of 1 to 7 days. The 60.5 kDa product in polyacrylamide corresponded to one of two polypeptides present in arylsulfatase A isolated from human placenta. In fibroblasts from a patient with metachromatic leukodystrophy no immune precipitable polypeptides of arylsulfatase A were detected. In normal fibroblasts less than 10% of the precursor of arylsulfatase A was secreted into the medium, whereas in mucolipidosis II fibroblasts and in control fibroblasts grown in the presence of NH4Cl up to 90% of the precursor of arylsulfatase A, appeared in the medium and remained there without change in the apparent molecular mass for at least 7 days. Arylsulfatase A polypeptides appear to contain two carbohydrate side chains. In about 90% of the polypeptides both side chains are cleaved by endo-beta-N-acetylglucosaminidase H, whereas in the remaining chains one of the two oligosaccharides is not cleaved.
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PMID:Synthesis and processing of arylsulfatase A in human skin fibroblasts. 612 36

The rhodizonic acid method for the determination of SO2-4 has been used to investigate the glycosulphatase activity of the sulphatase A (aryl-sulphate sulphohydrolase, EC 3.1.6.1) of ox liver. Sulphatase A hydrolyses D-glucopyranose and D-galactopyranose 2-, 3-, 4- and 6-sulphates: glucose sulphates are hydrolysed more rapidly than galactose sulphates and the 3-sulphates more rapidly than the other isomers. 2-Acetamido-2-deoxyglucopyranose 6-sulphate is not hydrolysed, nor is 2,3,4,6-tetra-O-acetyl-beta-D-glucopyranose 1-sulphate. Sulphate is a competitive inhibitor of the glycosulphatase activity. Hydrolysis proceeds through fission of the O-S bond. Evidence is given that the hydrolysis of glucose 3-sulphate is accompanied by the formation of substrate-modified sulphatase A, although this has not been isolated. Sulphatase A has no detectable alkylsulphatase activity.
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PMID:The sulphatase of ox liver. XXIV. The glycosulphatase activity of sulphatase a. 612 16


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