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 variant of metachromatic leukodystrophy (MLD), Austin disease, is characterized by a multiple isozyme deficiency of arylsulfatase. A 3 1/2-year-old girl with progressive mental and physical deterioration had decreased activities of arylsulfatases A and B in the leukocytes, shown by acylamide gel electrophoresis. Under the electron microscope, biopsy specimens of the brain and the peripheral nerve showed lamellar structures with socalled zebra bodies in the cytoplasmic processes of glial cells, granulo-membranous inclusions with fingerprint configurations in neurons, and myelinlike material in Schwann cells. Results from our study suggest an intricate nature of this dysmetabolic disorder, which shows ultrastructural changes usually seen in classic MLD, a deficiency of arylsulfatase A only, concomitant with those seen in mucopolysaccharidoses such as Hurler and Sanfilippo syndromes.
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PMID:Metachromatic leukodystrophy. Ultrastructural and enzymatic study of a case of variant O form. 0 Sep 85

The presence of hyaluronoglucosidase (EC 3.2.1.35; hyaluronidase), beta-N-acetylglucosaminidase (EC 3.2.1.30), exo-1,4-beta-xylosidase (EC 3.2.1.37), and arylsulfatase (EC 3.1.6.1) in dentinogenically active odontoblasts isolated from the rat incisor has been demonstrated by means of biochemical methods. The possible function of these enzymes in relation to the calcification process is discussed.
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PMID:Acid hydrolases in the odontoblast-predentin region of dentinogenically active teeth. 0 47

Arylsulfatase A and B activities were assayed in leucocytes of 43 controls, 11 cases of Metachromatic Leucodystrophy and 7 parents or siblings of patients, using a new technique implying specific inhibitors for leucocyte enzymes. Heterozygotes can be determined, with a 50% value compared to the control, in variant B. Electrophoresis of leucocytes after enzymatic staining for arylsulfatase, is a complementary technique which allowed the detection of a new form of metachromatic leucodystrophy.
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PMID:Arylsulfatases isoenzymes in metachromatic leucodystrophy/detection of a new variant by electrophoresis improvement of quantitative assay. 0 67

Mice from 12 inbred strains were surveyed for variation of kidney and liver arylsulfatase levels. Kidney variation was due to differences in the activity of arylsulfatase B. Twofold higher activities of arylsulfatase B in SWR/J kidney compared to A/HeJ kidney were determined by an autosomal gene which may be identical to the structural gene for arylsulfatase B since the SWR/J enzyme was more heat-stable than the A/HeJ enzyme. C57BL/6J mice possessed two-fold higher liver arylsulfatase levels than did A/HeJ mice. The major portion of this variation could be attributed to differences in arylsulfatase B, and appeared to be inherited in autosomal fashion. Although some evidence supports the existence of a major locus influencing liver arylsulfatase activity, this must be substantiated by further studies. Whatever the nature of the genetic factors involved, they do not appear to involve structural genes since no differences were discernible between the enzymes of the two strains relevant to Km, heat stability, electrophoretic mobility, pH optimum, activation energy, or response to several inhibitors. Furthermore, the rank ordering of strains on the basis of kidney arylsulfatase activity differed markedly from that which pertained to liver activity. Kidney arylsulfatase levels, but not brain or liver arylsulfatase activities, appear subject to androgenic influences.
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PMID:Genetics of murine liver and kidney arysulfatase b. 0 36

Optimal assay conditions are described for 8 hydrolases of Euglena gracilis var. bacillaris, SM-L1 (streptomycin-bleached) strain, 7 of which have an acid pH-optimum. Acid-phosphatase, beta-galactosidase, beta-glucosidase, b-fucosidase, cathepsin D, RNase, DNase, and an esterase are active in cell homogenates. Amylase has very low activity, and beta-glucuronidase, arylsulfatase, beta, N-acetyl-glucosaminidase, alpha-fucosidase, and alpha- and beta-mannosidase are inactive.
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PMID:Hydrolytic enzymes of Euglena gracilis: characterization and activity as a function of culture age and carbon deprivation. 0 4

Two glycosulfatases [EC 3.1.6.3], I and II, were purified 31.3- and 33.9-fold respectively, from a crude extract of the liver of Charonia lampas. The purification was carried out by the following chromatographic procedures; phosphocellulose, Sephadex G-150, Concanavalin A-Sepharose and isoelectric focussing. The enzyme preparations obtained were practically free from arylsulfatase [EC 3.1.6.1] contamination. Both glycosulfatases are probably glycoproteins differing in their carbohydrate moieties. The molecular weights of glycosulfatase I and II were estimated to be about 112,000 and 79,000 respectively. They had the same optimum pH of 5.5, and the same Km value of 25.0 mM for glucose 6-sulfate.
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PMID:Two glycosulfatases from the liver of a marine gastropod, Charonia lampas. Partial purification and properties. 0 53

It is known that the composition and character of human saliva alters during the menstrual cycle, presumably in response to changes in the level of ovarian hormones. A clinical study was undertaken to determine cyclic variations in salivary enzymes. Saliva from 4 healthy women aged 20-31 with a history of normal menstrual cycles were studied. The laboratory procedures performed on the saliva samples--from 6 menstrual cycles--are described and the results are graphed. Exfoliated cells from the oral mucosa were the main source of these enzymes. In all the cycles, alkaline phosphatase activity peaked sharply at mid-cycle, close to the expected time of ovulation; in 5 of the cycles, the peak occurred before the postovulation rise in body temperature. The levels of arylsulfatase and beta-glucuronidase, studied in 2 consecutive cycles of 1 woman, peaked in the periovulatory phase. All 3 enzymes were elevated during the luteal phase of the cycle as well. Increased cellular content of the saliva is attributed to the elevated circulating blood estrogen levels in the immediate preovulatory and midluteal phases of the cycles. There is great variability among subjects, however. Before a simple test for ovulation by home measurement of salivary enzymes can be developed, an ajustment of the test sensitivity would be necessary for adaptation to the individual woman.
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PMID:Alkaline phosphatase, arylsulfatase and beta-glucuronidase in saliva of cyclic women. 0 94

Slow reacting substance of anaphylaxis (SRS-A) was released from human lung passively sensitized with ragweed antibody and challenged with specific antigen E. After purification by ethanol extraction, incubation with alkali (0.1 M NaOH for 30 min at 37 degrees C) and chromatography on silicic acid and DEAE-cellulose, human SRS-A was separated into four biologically active fractions (Fractions I to IV). Arylsulfatase (Type H-1) in 0.1 M sodium acetate buffer, pH 4.5, destroyed the biologic activity of only Fraction I. All four fractions, like SO4=, inhibited the arylsulfatase activity at pH 4.5 but not at pH 6.0 when p-nitrocatechol sulfate was used as substrate. These results suggest that SRS-A contain a sulfur group and that human STS-A, like the prostaglandins, may be a family of compounds. The instability of the purified SRS-A to storage remains a major barrier to their further purification and chemical identification.
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PMID:Separation of slow reacting substance of anaphylaxis (SRS-A) from human lung into four biologically active fractions. 0 68

Cultured normal human articular cartilage chondrocytes exhibited decreasing levels of arylsulfatase A and B activities when grown in the presence of increasing levels of ascorbic acid (0 to 90 mug/ml) in the media. That this was not a general effect on all lysosomal enzymes was supported by the increase in acid phosphatase activity and no change in beta-glucuronidase activity observed with increasing levels of vitamin C under identical culture conditions. No decrease in either arylsulfatase activity was observed when ascorbic acid was replaced by ascorbate-2-sulfate. Ascorbic acid did not inhibit either arylsulfatase activity when added directly to the assay mixture. These data, combined with results of mixing experiments, suggest that the effect of vitamin C is mediated through cellular factors produced in response to its inclusion in the growth media.
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PMID:Effect of ascorbic acid on arylsulfatase A and B activities in human chondrocyte cultures. 1 Oct 78

Biotransformation of phenobarbital (PB) to p-hydroxyphenobarbital (PHPB) was studied quantitatively by gas-liquid chromatography in 8 epileptic patients who were receiving an established regimen of antiepileptic drugs including PB. PB and both conjugated and unconjugated PHPB were present in each patient's urine; m-hydroxyphenobarbital (MHPB) was not detected despite an assay sensitivity of 0.25 mug/ml. Incubation of the urine with beta-glucuronidase, but not with arylsulfatase, liberated PHPB which was, therefore, presumed to be conjugated with glucuronic acid. In general, the patients' urine contained more PB than total PHPB. Recovery of the patients' total daily dose of PB ranged from 24 to 77% (mean, 42%). After receiving a single iv dose of PB, PB and both conjugated and unconjugated PHPB were found in a normal volunteer's urine throughout a 16-day collection period; 30% of the dose was recovered. PB excretion was proportional to urine volume in the volunteer and in two additional patients who were made to vary their daily fluid intake. PHPB was not detected in the cerebrospinal fluid of 10 patients receiving PB. Neither PB, PHPB, nor MHPB were detected in the feces of four patients. These results suggest that metabolites other than PHPB or MHPB may be important in the elimination of PB in man.
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PMID:Metabolic fate of phenobarbital. A quantitative study of p-hydroxyphenobarbital elimination in man. 1 77


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