Arylsulphatases A and B in blood

Gniot-Szulzycka, J

doi:10.1016/0009-8981(71)90458-x

Cited by 12 publications

(5 citation statements)

References 10 publications

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“…The enzyme was completely retained on the column and could be eluted with 0.25M-NaCl. Similar results were obtained with arylsulphatase A from other sources (Bleszynski et al, 1969;Gniot-Szulzycka, 1972). SP-Sephadex chromatography gave 10-fold purification of arylsulphatase A, with 53 % recovery of enzyme activity over that in the previous step.…”

Section: Resultssupporting

confidence: 83%

Isolation, characterization and the role of rabbit testicular arysulphatase A in fertilization

Farooqui¹,

Srivastava²

1979

Biochemical Journal

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Arysulphatase A was purified from rabbit testis. The purification was accomplished by a four-step procedure involving (NH4)2SO4 fractionation, chromatography on DEAE-cellulose, SP(sulphopropyl)-Sephadex and affinity chromatography on concanavalin A-Sepharose. The specific activity of purified preparation was 135 mumol/min per mg of protein, which represented an increase of 900-fold above that of the crude homogenate. The purified enzyme (20-50 micrograms) was found to move electrophoretically as a single band on polyacrylamide gel at pH 7.2 and 8.4. The homogeneous enzyme was shown to be a glycoprotein with 0.8% (w/w) of N-acetylneuraminic acid and 20% neutral sugar. The treatment of purified enzyme with bacterial neuraminidase had no effect on enzyme activity or kinetic properties, but it changed the elution prolife of rabbit testis arylsulphatase A through DEAE-Sephadex. The purified enzyme was strongly inhibited by Cu2+, Fe3+ and Ag+. It hydrolysed several sulphate esters including cerebroside 3-sulphate, ascorbic acid 2-sulphate and steroid sulphates. Pure arysulphatase was effective in dispersing the cumulus cells of rabbit ova.

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Section: Resultssupporting

confidence: 83%

Isolation, characterization and the role of rabbit testicular arysulphatase A in fertilization

Farooqui¹,

Srivastava²

1979

Biochemical Journal

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“…Accordingly, our finding concerning the increased ARS-A activity in reproductive phases when endogenous steroid hormones are highly influential, is in agreement with earlier findings which reported steroid hormone-induced increases in ARS's in different animals (Vitaioli, Menghi and Baldoni 1984;Vitaioli et al 1985a;Vitaioli, Baldoni and Sanguini 1985b;Vitaioli, Baldoni, Bellini, Pederzoli and Bolognani 1988). Similarly, an earlier report of increased ARS-A activity in the serum of pregnant women tends to support the hypothesis that physiological increases in gonadal steroids could have a stimulating effect on ARS-A activity (Gniot-Szulzycka 1971).…”

Section: Discussionsupporting

confidence: 58%

Relationship of Some Endogenous Sex Steroid Hormones to Leukocyte Arylsulphatase A Activities in Pre- and Postmenopausal Healthy Women

Öner

Bekpınar²,

Cinar³

et al. 1994

Horm Metab Res

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This study was planned to investigate whether the physiological variations in endogenous gonadal steroid hormones during fertile period to menopause might affect the Arylsulphatase A (ARS-A) activities in leukocytes in healthy women. In premenopausal women, means of the leukocyte ARS-A activity were significantly highest at ovulatory phase, and lowest at early follicular phase. In contrast, the mean leukocyte ARS-A activity in postmenopausal women was approximataely equivalent to the mean leukocyte enzyme in cycling women at early follicular phase in whom the lowest enzymatic activity was observed. The results of our study, therefore, concluded that gonadal steroid released physiologically into the bloodstream might be expected to stimulate the lysosomal system thereby leading to an enhancement in leukocyte ARS-A activity.

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“…Both ox liver (Nichol & Roy, 1965) and rat tissue arylsulphatases exist as a tetramer at pH 5.0. Human placenta arylsulphatase A exists as a monomeric form at pH5.0 and 7.5, as estimated by thin-layer gel filtration (Gniot-Szulzycka, 1974). Two arylsulphatases from human brain, that are absorbed and excluded on DEAE-cellulose, have apparent mol.wts.…”

Section: Discussionmentioning

confidence: 99%

Purification and properties of arylsulphatase A from rabbit testis

Yang¹,

Srivastava²

1976

Biochemical Journal

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Rabbit testis arylsulphatase A was purified 140-fold with a recovery of20 % from detergent extracts of an acetone-dried powder by using DE-52 cellulose column chromatography, gel filtration on Sephadex G-200 and preparative isoelectric focusing. The purified enzyme showed one major band with one minor contaminant on electrophoresis in a 7.5% (w/v) polyacrylamide gel at pH 8.3. On sodium dodecyl sulphate/polyacrylamidegel electrophoresis, a single major band was observed with minor contaminants. The final preparation of enzyme was free from general proteolytic, esterase, hyaluronidase, A6-glucuronidase and fi-galactosidase activities. Rabbit testicular arylsulphatase A exists as a dimer of mol.wt. 110000 at pH7

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Arylsulphatases A and B in blood

Cited by 12 publications

References 10 publications

Isolation, characterization and the role of rabbit testicular arysulphatase A in fertilization

Isolation, characterization and the role of rabbit testicular arysulphatase A in fertilization

Relationship of Some Endogenous Sex Steroid Hormones to Leukocyte Arylsulphatase A Activities in Pre- and Postmenopausal Healthy Women

Purification and properties of arylsulphatase A from rabbit testis

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