Results 221 to 230 of about 14,004 (249)

Characterization of human arylsulfatase a glycans

International Journal of Biochemistry, 1994
Despite numerous studies on arylsulfatase A, the structure of the glycans present in each of its two subunits has not been determined. This is important because the carbohydrate component of human arylsulfatase A synthesized in tumor tissues and transformed cells has been shown to undergo apparent changes.
P, Laidler, A, Litynska, M, Galka-Walczak, B, Wojczyk   +3 more
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A Km mutant of arylsulfatase A

Clinica Chimica Acta, 1982
Abstract The apparent Michealis constant for p-nitrocatechol sulfate of arylsulfatase A of fibroblasts of a metachromatic leukodystrophy patient has been determined and compared to that of normal controls. Control cells gave an apparent Km of 0.7 mmol/l, while the apparent Km of patient's cells was determined to be 19.8 mmol/l.
A M, Harben, N, Krawiecki, R, Marcus, F A, Hommes   +3 more
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Interstrain variation of murine arylsulfatase C

Experientia, 1979
A method has been developed for the assay of arylsulfatase C in tissue extracts containing arylsulfatases A and B. Significant variation of enzyme activity was observed among 26 inbred murine strains. Activity differences were apparent at all stages evaluated between 1 and 70 days postnatal age.
Nelson, K, Daniel, W L
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Arylsulfatases in bilharziasis.

Egyptian journal of bilharziasis, 1978
Arylsulfatase A and B in urine have been estimated in 18 normal subjects and 50 bilharziasis patients. The bilharziasis patients were divided into two groups according to the type of infeciton. Those with bilharziasis haematobian type of infection and those with the bilharziasis mansoni type.
E Z, Khafagy, H E, Raziky, A F, Galal
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Specific determination of arylsulfatase A activity

Experientia, 1986
Arylsulfatase activities in biological materials are too low to be detected by the methods available hitherto. A sensitive and specific assay method for arylsulfatase A (AS-A) has been developed in the present study. Ascorbate-2-sulfate is known to be a specific natural substrate of AS-A; the ascorbic acid liberated by the action of AS-A was ...
H, Inoue, Y, Seyama, S, Yamashita
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Comparative studies of rodent anionic arylsulfatases

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1985
Approximately 25 and 40%, respectively, of murine (Mus musculus) and rat (Rattus norvegicus) hepatic arylsulfatase (EC 3.1.6.1) activity eluted from DEAE-ion exchange resins under high salt conditions. This high salt fraction contained arylsulfatase A and an enzyme which was immunologically similar to arylsulfatase B. The latter enzyme was thermostable,
D B, Thompson, W L, Daniel, J H, Glaser
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Arylsulfatases: Colorimetric and fluorometric assays

1987
Publisher Summary This chapter discusses the colorimetric and fluorometric assays of arylsulfatases. The assay of arylsulfatases is simple in principle, and any of the reaction products may be determined. The general method is simple and requires only that the reaction mixture, after incubation with the enzyme, be made alkaline so that the liberated ...
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Bestimmung der Arylsulfatase-Aktivität

1991
Bodenproben werden nach Zusatz einer p-Nitrophenylsulfatlosung 1 Stunde bei 37°C inkubiert. Das enzymatisch abgespaltene Nitrophenol wird mit Natronlauge angefarbt und bei 420 nm photometrisch bestimmt.
Franz Schinner, Richard Öhlinger, Ellen Kandeler   +2 more
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Arylsulfatase A Pseudodeficiency - Incidence in Poland

European Journal of Human Genetics, 1996
Arylsulfatase A (ASA) pseudodeficiency (Pd) was defined as the in vitro measurement of low enzyme activity in a healthy person. A variable incidence of the Pd allele was found in different populations; it was 10-20 times higher than that of metachromatic leukodystrophy (MLD).
B, Czartoryska, J G, Zimowski, M, Bisko, D, Górska   +3 more
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Arylsulfatase multiplicity in Proteus rettgeri

Canadian Journal of Microbiology, 1970
Multiple electrophoretic species of arylsulfatase were demonstrated in sonicates of Proteus rettgeri by paper electrophoresis. Subsequent treatment of the sonicates with streptomycin sulfate and DEAE-cellulose chromatography resolved enzyme activity into four fractions.
J W, Fitzgerald, F H, Milazzo
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