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Arylsulfatase activity

Studies on the fate of dopamine 4-sulfate (9.88) will serve to illustrate the reaction of deconjugation mentioned above. With this substrate, arylsulfatase activity in the dog was found to be highest in the kidney and liver, low in the intestine and heart, and almost nil in the brain and skeletal muscle [171]. Since this conjugate exists in high amounts in the plasma of humans, monkeys and dogs, the possibility was raised that it might be looked upon as a precursor or reservoir of free dopamine. [Pg.595]

Figure 4. Arylsulfatase activity ( - ) and sulfotransferase activity (a-a) in developing larvae of the southern armyworm (. eridania). Figure 4. Arylsulfatase activity ( - ) and sulfotransferase activity (a-a) in developing larvae of the southern armyworm (. eridania).
Histochemical observations. There was an increase in acid phosphatase and arylsulfatase activity in the region of basal epidermal cells, reaching a maximum at 3 h post-exposure. This was attributed to activation of lysosomal enzymes. At 8 and 19 h, post-exposure increased arylsulfatase staining of fibroblasts and histiocytes was noted. At 19 h, clusters of large AT-Pase positive mononuclear cells were identified just below the epidermis. These may have been derived from the Langerhans cells of the antigen presenting series. [Pg.390]

Dzialozynski, L. M., and Gniot-Szulzycka, J., Some chnical aspects of arylsulfatase activity. [Pg.190]

French, A. P., and Warren, J. C., Properties of steroid sulfatase and arylsulfatase activities of human placenta. Biochem. J. 105, 233-241 (1967). [Pg.192]

Higuchi, M., Nishio, T., Ichiki, M., Tsuda, S., and Sasai, Y. Arylsulfatase activity in blister fluids of bullows pemphigoid. Nishinihon ]. Dermatol. 44, 405-408 (1982). [Pg.193]

Kresse, H, and Holtfrerich, D., Thiosulfate-mediated increase of arylsulfatase activities in multiple sulfatase deficiency disorder fibroblasts. Biochem. Biophys. Res. Commun. 97, 41-48 (1980). [Pg.195]

Shapira, E., and Nadler, H. L., The nature of the residual arylsulfatase activity in meta-chromatic leukodystrophy. J. Pediatr. 86, 881-884 (1975b). [Pg.199]

Arylsulfatase activity is usually measured with the chromogenic substrate 4-nitrocatecholsulfate. (A fluorogenic substrate, 4-methylumbelli-ferylsulfate, is also available but is less frequently used because it is hydrolyzed only very slowly.) The assay system of Baum et al. (1959), which was developed to permit the determination of arylsulfatase A in the presence of the B isoenzyme, is still most widely used. The unusual time course of the hydrolysis of 4-nitrocatecholsulfate by arylsulfatase A (Roy, 1953 Baum et al., 1958 Stinshoff, 1972) may present a problem for standardization of the enzyme preparation and should be taken into account, such as by using short incubation times (15-30 min). The enzyme unit is usually defined as the amount of enzyme that hydrolyzes 1 p.mol of this substrate per minute. [Pg.10]

Chen, C.R., Condron, E.M., Davis, M.R. and Sherlock, R.R. (2001) Effects of land-use change from grassland to forest on sulfur availability and arylsulfatase activity in New Zealand. Australian Journal of Soil Research 39, 749-757. [Pg.304]

LTD, to corresponding E leukotrienes [114,130,221], This enzyme has been partially purified from kidney [130], human plasma [128], RBL cells, guinea pig lung, and guinea pig peritoneal eosinophils [104], In the latter preparations, the peptidase activity could be resolved from the arylsulfatase activity [104], which had earlier been suggested to be responsible for inactivation of SRS [101,102], Inhibitors of the dipeptidase, more potent than L-cysteine, are 3-mercaptopropionic acid and D-peni-cillamine [114],... [Pg.141]

In some patients, exhibiting symptoms of the juvenile type of metachromatic leukodystrophy, the disease is caused by a defect in saposin B, an activator that is necessary for full arylsulfatase activity [2]. [Pg.432]

In 1963, Mehl and Jatzkewitz succeeded in isolating fractions with cerebroside-sulfatase activity from pig kidneys, and Bleszynski and Dzialoszynski (1965) purified soluble arylsulfatases from ox brain. A study by Mehl and Jatzkewitz (1965) on the significance of a lack of arylsulfatase in ML as reported by Austin (1963 a), and Austin et al. (1964 a, b), with 2-hydroxy-5-nitrophenyl-sulfate as substrate, resulted in the finding of two fractions with arylsulfatase activity in normal kidneys. While in ML the smaller of both fractions was present in normal concentration, the second component, and the predominant one in normals, was below the limits (0.005 o. d. units Mehl and Jatzkewitz 1965) of the method in ML. It seems that diminution or lack of this heat-labile fraction, which corresponds to the arylsulfatase A of Austin, is typical for ML, and according to Mehl and Jatzkewitz (1965), supports the assumption of a block in the degradation of ML between sulfatides and cerebrosides (see fig. 3). [Pg.326]

AL-KHAFAJl A.A. and TABATABAI M.A. 1979. Effects of trace elements on arylsulfatase activity in soils. Soil Science, 127, 129-133. [Pg.213]

TABATABAI M.A. and BREMNER J.M. 1970. Factors affecting soil arylsulfatase activity. Soil Science Society of America Proceedings, 427-429. [Pg.220]

Multiple sulfatase deficiency (MSD). The clinical presentation of MSD includes features of MLD and the MPS, with the features that resemble MLD, such as gait disturbances, psychomotor retardation and polyneuropathy predominating. MPS-like features, such as facial coarsening, hepatosplenomegaly and joint stiffness, are present to a milder and variable extent. A reduction in the activity of all sulfatases is the key diagnostic abnormality. Von Figura and associates have demonstrated that catalytic activity of all sulfatases requires a post-translational modification in which a cysteine residue (cysteine 69 in arylsulfatase A) is oxidized to an aldehyde. It is this modification that is defective in MSD [5]. [Pg.688]

Enzyme activity (urease, amidase, dehydrogenase, pl-glucosidase, phosphatase, arylsulfatase, fluorescein diacetate hydrolysis) Laboratory incubation Indicates potential microbial activity and nutrient cycling reactions determined in nonstandard laboratory with specialized equipment highly spatially and temporally variable dependent upon organic inputs Dick et al. (1996) Parham et aL (2002)... [Pg.283]

Patients with multiple sulfatase deficiency also show low N-acetylglucosamine-6-sulfatase activity. Therefore, arylsulfatase A or another sulfatase should also be determined in case of low results for a single sulfatase, especially when jS-galactosidase activity is in the normal range for that sample. [Pg.315]

The activity is calculated using the standard curve and the result for the absorption (patient) because during the first 30 min of incubation some of the activity may be derived from arylsulfatase A instead of arylsulfatase B. Results are expressed in nmol/ mg protein-h. [Pg.319]

In case of a deficiency of arylsulfatase A, at least one other sulfatase should be measured to exclude multiple sulfatase deficiency (see Chap. 4.1 for the assays of arylsulfatase and other sulfatases). Sulfatide excretion in urine should be measured (see assay below) and/or mutation analysis should to performed to confirm the diagnosis, especially if the clinical symptoms are atypical and in order to exclude a pseudodeficiency of arylsulfatase A. The enzyme should always be measured in the parents to check for the presence of compound heterozygosity of a metachromatic leukodystrophy and a pseudodeficiency allele. This is very important for the interpretation of the results of arylsulfatase A assays, especially when performed in asymptomatic or presymptomatic siblings or in the context of a prenatal diagnosis. Sulfatide should also be measured in case a normal arylsulfatase A activity is found in a patient with symptoms characteristic of (juvenile) metachromatic leukodystrophy. Increased urinary sulfatide excretion is indicative of an activator protein/saposin deficiency (Fig. 4.4.1). [Pg.366]

Leinekugel P, Michel S, Conzelmann E, Sandhoff (1992) Quantitative correlation between the residual activity of beta-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage disease. Hum Genet 88 513-523... [Pg.376]

Wenger DA, Louie E (1991) Pseudodeficiencies of arylsulfatase A and galactocerebrosidase activities. DevNeurosci 13 216-221... [Pg.378]

Reiter et al. (43) have shown that a second enzyme can also act to degrade SGG. They found that secondary lysosomes from rat liver contained not only arylsulfatase A, but also a lipase activity that could act to de-acylate SGG. Under the conditions used, more product was formed by the action of the lipase on SGG than by the action of arylsulfatase A. These workers also found that the latter enzyme could use the lyso-SGG as a substrate. It would be... [Pg.113]

Cadmium in the body is known to affect several enzymes. It is believed that the renal damage that results in proteinuria is the result of cadmium adversely affecting enzymes responsible for reabsorption of proteins in kidney tubules. Cadmium also reduces the activity of delta-aminolevulinic acid synthetase (Figure 10.3), arylsulfatase, alcohol dehydrogenase, and lipoamide dehydrogenase, whereas it enhances the activity of delta-aminolevulinic acid dehydratase, pyruvate dehydrogenase, and pyruvate decarboxylase. [Pg.234]

Arylsulfatase cleaves sulfate esters. Cerebroside sulfate is its natural substrate. The enzyme is also active toward p-nitrocatechol sulfate, which is the basis for this assay. [Pg.224]

Arylsulfatase B catalyzes the hydrolysis of the sulfate from UDP-Gal-NAc-4-sulfate to form UDP-GalNAc and sulfate. This activity is found in normal fibroblasts but not in Maroteaux-Lamy fibroblasts. [Pg.285]

The HPLC method has been used to assay a number of activities usually found associated with lysosomal vesicles. All these assays utilize the fluorometric compound 4-methylumbelliferone (4-MU). When carbohydrates, lipids, phosphates, or sulfates are conjugated with 4-MU, these compounds can be used as substrates for glycosidase, lipases, acid phosphatases, and arylsulfatases. The activity is determined by the release of 4-MU. [Pg.291]

Studies on the activity of rabbit sperm acrosomal enzymes have indicated that gossypol at 12-76 pM could significantly inactivate azocoll proteinase, acrosin, neuraminidase, and arylsulfatase. Hyaluronidase, p-glucuronidase, and acid phosphatase were also inhibited at a higher concentration of gossypol (380 pM) (Yuan et al., 1995). Since acrosomal enzymes play important roles in the fertilization process, the inhibition of... [Pg.236]

Cserfalvi and Guilbault (1976) developed a sensor for the measurement of sulfate by using aiylsulfatase (EC 3.1.6.1). Arylsulfatase catalyzes the hydrolysis of arylsulfates under formation of an electrode-active product ... [Pg.261]


See other pages where Arylsulfatase activity is mentioned: [Pg.394]    [Pg.52]    [Pg.411]    [Pg.196]    [Pg.632]    [Pg.488]    [Pg.213]    [Pg.394]    [Pg.52]    [Pg.411]    [Pg.196]    [Pg.632]    [Pg.488]    [Pg.213]    [Pg.6]    [Pg.354]    [Pg.113]    [Pg.116]    [Pg.349]    [Pg.232]    [Pg.213]    [Pg.416]    [Pg.286]    [Pg.210]    [Pg.134]    [Pg.412]   
See also in sourсe #XX -- [ Pg.234 ]




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