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)

An ammonium sulfate-precipitated fraction from cell-free extracts of Pseudomonas C12B grown on a medium containing sodium dodecyl sulfate (SDS) contained alkyl sulfatase increased fourfold in specific activity over the crude. Optimal pH (7.5) and temperature (70 C) for sulfate release were determined with SDS labeled with radioactive sulfur (SDS(35)) as test substrate. Phosphate, arsenate, and certain heavy metal ions inhibited desulfation, whereas Mg(++) and Mn(++) stimulated activity of preparations which had been dialyzed against ethylenediaminetetraacetic acid. Dodecanol was recovered in semiquantitative yield from reaction mixtures containing enzyme and SDS(35). Aryl sulfates, secondary alcohol sulfates, and a phenoxyethyl sulfate failed to serve as substrate for this enzyme.
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PMID:Primary alcohol sulfatase in a Pseudomonas species. 586 50

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

A rapid capillary GLC method for the analysis of conjugated estrogen tablets and injectable formulations is described. The method involves the hydrolytic cleavage of the sodium sulfate ester conjugates by sulfatase enzyme. The free phenolic steroids are reacted sequentially with hydroxylamine hydrochloride and N,O-bis(trimethylsilyl)trifluoroacetamide. The resulting dual derivatives are analyzed on a 15-m glass capillary column wall coated with a cyanopropylmethyl silicone phase.
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PMID:Quantitative determination of conjugated estrogens in formulations by capillary GLC. 610 Dec 18

A simple assay technique for the determination of sulfatidase activity in leukocytes has been developed for the reliable diagnosis of metachromatic leukodystrophy (MLD). Sulfatide is tritiated in sphingosine and fatty acid by reduction with [3H]sodium borohydride in alkali in the presence of palladium chloride. This labeled natural substrate for aryl sulfatase A (AsA) is hydrolyzed by normal human leukocytes in 25 mM-acetate buffer, pH 5.0, in the presence of 0.3% sodium taurodeoxycholate. The enzyme activity is greatly improved after dialysis, exhibiting better linearity with protein concentration. It is stimulated maximally by 5 mM-MnCl2 with an apparent Km of 0.17 mM for the substrate. Patients with MLD exhibited virtually no detectable sulfatidase activity although they had residual AsA activity that was measured with the synthetic substrate, p-nitrocatechol sulfate (NCS). Potential heterozygotes could be identified by the sulfatidase assay in instances where the NCS assay for AsA was inconclusive. Several individuals with levels of AsA activity characteristic of MLD, including a few healthy carriers and certain patients with unknown neurological diseases, were shown not to have MLD by the presence of measurable levels of sulfatidase in their leukocytes.
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PMID:Leukocyte sulfatidase for the reliable diagnosis of metachromatic leukodystrophy. 610 67

Analysis of arylsulfatase A from pseudo arylsulfatase A deficiency fibroblasts by sodium dodecyl sulfate polyacrylamide gel electrophoresis and immunoradiochemical nitrocellulose blot radiography revealed two subunit bands which migrated faster than subunit bands of enzyme from normal fibroblasts. Immunoreactive material was present only at levels comparable to enzyme activity. These findings imply that arylsulfatase A in pseudodeficiency is structurally altered, but it is catalytically equivalent to normal arylsulfatase A. This altered enzyme must be the product of the pseudodeficiency gene since no immunoreactive product of the metachromatic leukodystrophy gene could be detected in metachromatic leukodystrophy cells by the procedure employed. It is not clear from the present data if the attenuated arylsulfatase A activity in pseudodeficiency results from a decreased rate of synthesis or an increased lability of the mutant enzyme.
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PMID:Pseudo arylsulfatase A deficiency: evidence for a structurally altered enzyme. 613 5

A large portion of the dose of propranolol in animals and man is unaccounted for. Using radiotracer and HPLC techniques, five previously unrecognized polar and labile metabolites were found in dog urine, together accounting for 34% of the urinary radioactivity. The two main metabolites, peak 2 (7% of the radioactivity) and peak 4 (17%) could be isolated and purified by butanol extraction and reversed phase HPLC. Direct probe MS analysis of the main peak 4 and GC/MS analysis of the same peak after trifluoroacetylation both yielded 4-hydroxypropranolol. These observations together with UV spectra before and after acid hydrolysis indicated peak 4 to be an acid- and heat-labile conjugate of 4-hydroxypropranolol with the conjugating group at the phenolic oxygen atom. Arylsulfatase from Helix pomatia and Aerobacter aerogenes completely hydrolyzed peak 4 to 4-hydroxypropranolol. Urine and plasma as well as the antioxidant sodium bisulfite, however, markedly inhibited the arylsulfatase activity. After conversion of peak 4 to its sodium salt, a fast atom bombardment-positive ion mass spectrum confirmed this metabolite to be the sulfate ester of 4-hydroxypropranolol, clearly demonstrating the quasimolecular ion (M + H)+ at m/z 378 as well as fragmentation with loss of the sulfate moiety. The second largest unknown metabolite in the dog, peak 2, was identified as the sulfate ester of 4-hydroxypropranolol glycol. The 4-hydroxypropranolol sulfate was also identified in both urine and plasma of a patient treated with propranolol, accounting for approximately 18% of the dose.
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PMID:Identification of major sulfate conjugates in the metabolism of propranolol in dog and man. 613 41

Cerebroside sulfatase (CSase) activator was isolated from human liver by acetone precipitation, anion-exchange chromatography, gel filtration and polyacrylamide gel electrophoresis. The CSase activator was a heat-stable protein with an isoelectric point of 4.54. Molecular weight (Mr) of the activator was estimated as 22,000 with the gel permeation and about 8,000 by gel electrophoresis in the presence of sodium dodecyl sulfate, suggesting that the native activator is a trimer of a subunit with Mr 8,000. The CSase activator formed a complex with an equimolar amount of cerebroside sulfate (CS), when examined by gel permeation experiments. The activator also bound to galactosylceramide and GM2 ganglioside but scarcely to GM1 ganglioside, and activated to some extent beta-N-acetyl-hexosaminidase A and beta-galactosidase, although the CSase activator could be clearly distinguished from the GM1 beta-galactosidase activator so far known. Though the affinity chromatography using glycolipid ligands, the CSase activator did not recognize sulfate group of CS, but appeared to have a relatively broad specificity for lipid-linked hexose.
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PMID:[Purification and characterization of cerebroside sulfatase activator]. 614 Nov 30

Arylsulfatase A was purified from human lung to apparent homogeneity as determined by electrophoresis in the presence of sodium dodecyl sulfate. The enzyme from normal lung as well as that from lung adenocarcinoma showed considerable microheterogeneity when examined by isoelectric focussing, with an isoelectric point (pI) ranging from 5.1 to 4.6. The tumor enzyme was more heterogeneous and contained more acidic components than the normal lung enzyme. The cause of the charge heterogeneity was examined by treatment with exogenous hydrolases. Upon treatment with sialidase, phosphatase or endo-beta-N-acetylglucosaminidase H (endoglycosidase H), the acidic enzyme forms shifted to an alkaline region on isoelectric focussing gels. Combined treatment of the arylsulfatase A with endoglycosidase H and sialidase resulted in complete loss of the most acidic components to give the less acidic components with pI 5.1, 5.0, and 4.9. These results strongly suggest that the charge heterogeneity of arylsulfatase A is due not only to sialylation but also to phosphorylation at the carbohydrate moiety of the enzyme, and the extent of substitution by acidic groups is markedly increased in the tumor enzyme.
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PMID:Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. 614 14

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

Arylsulphatase C (EC 3.1.6.1) has been purified 300-fold from human placental microsomes using a four step procedure involving solubilization with Triton X-100, chromatography on hydroxyapatite, column chromatofocussing and ion-exchange chromatography on DEAE-Sepharose. The purified enzyme is electrophoretically homogeneous and has a molecular weight of 440 000 as determined by polyacrylamide gradient gel electrophoresis. On analysis of the preparation by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate a polypeptide of molecular weight 74 000 was observed, suggesting that the enzyme as purified may be a hexamer. The behaviour of the enzyme during chromatofocussing indicates the enzyme has a pI of 6.56. Steroid sulphatase, as measured by activity towards dehydroepiandrosterone sulphate, co-purifies with arylsulphatase C suggesting that both activities are due to a single enzyme.
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PMID:Purification and partial characterization of arylsulphatase C from human placental microsomes. 657 10


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