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)

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.
J Immunol 1976 Sep
PMID:Separation of slow reacting substance of anaphylaxis (SRS-A) from human lung into four biologically active fractions. 0 68

The enzyme liberated by some treatments and the changes in arylsulfatase C activity in chronic hepatic damage were investigated in rat liver. 1. The enzyme activity liberated by ultrasound was the highest in the conditions studied. 2. Arylsulfatase C was assayed using p-nitrophenyl sulfate in 0.25 M Tris/acetate buffer as substrate. It is shown that this method can be used to measure arylsulfatase C activity in a mixture of arylsulfatases A and B. 3. The enzyme is mainly located in the microsomal fraction in rat liver. In toxic hepatic damage, the enzyme activity decreases from the early stage; decreasing markedly in chronic hepatic damage. The activity seems to reflect damage to the microsomes and therefore arylsulfatase C activity can be a good indicator of injury to liver microsomes.
Clin Chim Acta 1976 Sep 20
PMID:Degradation of arylsulfate by hepatic microsomes. 0 16

To see whether urine enzyme activities could be used as an index in evaluating the disease status of leukemia patients, we examined the activities of four enzymes: arylsulfatases A(AS-A) and B(AS-B), alkaline phosphatase (AP), and lactate dehydrogenase (LDH). AP and LDH showed no consistent patterns. The activities of AS-A and AS-B correlated well with the patient's clinical status, increasing during progression of disease and decreasing toward normal activities during responses to therapy, as judged from bone marrow cellularity and differential. Among 23 untreated patients with a histologic diagnosis of acute leukemia we found increased activities of the urine enzymes in these proportions: AS-A in 23 patients (100%), AS-B in 22 (95.7%), AP in 7 (30.4%), and LDH in 10 (43.5%). Five patients in remission from acute leukemia had normal activities for all four enzymes. In one patient in remission for more than one year, a rise in urinary arylsulfatase activity preceded observable bone marrow relapse by 4 months. Unlike that of serum of urine lysozyme and serum copper, the determination of urine arylsulfatase activities appears to be a consistent, useful indicator of response to antileukemic therapy. In contrast to the determination of polyamines, the quantitation of arylsulfatase activity is achieved with greater ease and with instrumentation available in most clinical laboratories.
Cancer 1979 Sep
PMID:A noninvasive technique for monitoring response to chemotherapy in human acute leukemia. 3

Antibodies against homogeneous rabbit liver arylsulfatase A (aryl-sulfatase sulfohydrolase, EC 3.1.6.1) were produced in a goat and the effects of these antibodies on the kinetic parameters of the enzyme have been studied. The results indicate that the binding of antibody to the enzyme does not alter the enzyme active site, since Km and -ki values are unaffected. However, a small reduction in the enzyme activity was observed as the result of a reduction of V in the enzyme-antibody complex. The binding of antibodies led to a change in the pH-rate profile, giving one broad pH optimum shifted toward higher pH value. The enzyme-antibody complex still showed the characteristic arylsulfatase A anomalous kinetics at pH 5.5, but the inactivation was significantly slower than for the native enzyme. As calculated from quantitative immuno-precipitation data, the native enzyme bound 5--7 molecules of IgG. The number of IgG molecules which bound to the turnover-modified enzyme was reduced to 3--4. The loss of antigenic determinants from the turnover-modified enzyme indicates that significant conformational changes occur during the turnover-induced modification, or that a covalent modification of residues present at the antigenic sites has occurred, or both.
Biochim Biophys Acta 1979 Sep 12
PMID:Antigen-antibody interactions and the anomalous kinetics of arylsulfatase A. 3 7

It has been observed that multiple sulfatase deficiency disorder (MSDD) fibroblasts contained from profoundly deficient to near normal amounts of arylsulfatase (ARS) A depending on the medium in which they were cultured. Our present findings show that the major factor determining the enzyme level is the pH of the medium during growth. In media which became acidic or was maintained at low pH (less than 7), the cells expressed the enzymopathy, while in high pH media (7.4), the cells produced enzyme. The high and low enzyme states were reversible. The ARS A deficiency in MSDD must, therefore, be a secondary manifestation of a mutation in another system.
Am J Hum Genet 1979 Sep
PMID:Arysulfatase A modulation with pH in multiple sulfatase deficiency disorder fibroblasts. 4 50

A method for simultaneous quantitation of nine steroids in cord plasma is described which consists of Amberlite XAD-2-column chromatography at constant temperature of 45 degrees C, enzyme hydrolysis with beta-glucoronidase/aryl sulfatase, addition of five radioactive internal standards, ethyl acetate extraction, thin layer chromatography and quantitation by gas-liquid chromatography after trimethylsilyl ether derivative formation. Reliability criteria are established and the following steroid concentrations found: progesterone, 132.1 +/- 102.5 mug/100 ml; pregnenolone, 57.3 +/- 45.7 mug/100 ml; dehydroepiandrosterone, 46.5 +/- 29.4 mug/100 ml; pregnanediol, 67.5 +/- 46.6 mug/100 ml; 16-ketoandrostenediol 19.8 +/- 13.7 mug/100 ml; 16 alpha-hydroxydehydroepiandrosterone, 126.3 +/- 86.9 mug/100 ml; 16 alpha-hydroxypregnenolone, 78.2 +/- 56.5 mug/100 ml; androstenetriol, 22.2 +/- 17.5 mug/100 ml and oestriol, 127.7 +/- 116.9 mug/100.
Endocrinol Exp 1975 Sep
PMID:Method for the quantitation of steroids in umbilical cord plasma. 12 58

A simple and rapid method for the purification of arylsulfatase A (EC 3.1.6.1) from sheep brain has been developed. This includes the concanavalin A-Sepharose affinity chromatography and the pH-dependent polymerization and depolymerization of the enzyme. By these methods a homogeneous enzyme was obtained and the enzyme was purified 7180-fold. Sheep brain arylsulfatase A has been shown to be a glycoprotein containing 25% neutral sugar and 0.5% sialic acid. The constituent neutral sugars were identified as glucose and mannose.
Biochim Biophys Acta 1975 Sep 22
PMID:Purification, properties and glycoprotein nature of arylsulfatase A from sheep brain. 24 Apr 23

Praziquantel, a new anthelmintic drug with activity against all species of schistosomes pathogenic to man, and against a wide range of Cestodes, was tested for mutagenic potential. For the detection of both base substitutions and frameshift mutations, Salmonella typhimurium TA 100 and TA 98 were used as tester strains. Using the plate assay with and without added S-9, host-mediated assay and urine-mediated assay without and after incubation with beta-glucuronidase/arylsulfatase, no mutagenic activity could be detected.
Arch Toxicol 1977 Sep 28
PMID:Mutagenicity studies with praziquantel, a new anthelmintic drug: tissue-, host-, and urine-mediated mutagenicity assays. 33 17

Incubation of dopamine-4-O-sulfate with purified bovine dopamine-beta-hydroxylase led to the formation of free norepinephrine. The production of free norepinephrine was completely inhibited in the presence of 5.6 mM of fusaric acid, an inhibitor of dopamine-beta-hydroxylase. No sulfatase activity was detected in the incubation medium. The reaction of dopamine-4-O-sulfate with dopamine-beta-hydroxylase followed Michaelis-Menten kinetics, showing an apparent Km of 2.6 mM.
Can J Biochem 1979 Sep
PMID:Dopamine-4-O-sulfate: a possible precursor of free norepinephrine. 50 57

1. The activities of the three arylsulphatases (arylsulphate sulphohydrolase, EC 3.1.6.1) of Aspergillus oryzae produced under a variety of repressing and non-repressing conditions were determined. 2. These enzymes exhibit different sensitivities to repression by inorganic sulphate. 3. Arylsulphatase I, but not arylsulphatases II and III, exhibits a transient de-repression in the early growth phase in sulphate media. 4. When the fungus is cultured in repressing media and subsequently transferred to non-repressing media, the synthesis of the three enzymes is non-co-ordinate. 5. Growth of the fungus in media containing choline O-sulphate or tyrosine O-sulphate as the sole source of sulphur results in complete de-repression of arylsulphatase I, But the synthesis of arylsulphatases II and III is essentially fully repressed. 6. The marked similarities between the repression characteristics of arylsulphatases II and III, contrasted with those of arylsulphatase I, indicate that the genetic locus of arylsulphatase I is distinct from that of arylsulphatases II and III, suggesting that there are distinct physiological roles for the enzyme.
Biochem J 1977 Sep 15
PMID:Differential repression of arylsulphatase synthesis in Aspergillus oryzae. 59 36


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