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KMID : 0380219840170020120
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Journal of Biochemistry and Molecular Biology
1984 Volume.17 No. 2 p.120 ~ p.132
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Hwang In-Hwan
Yang Chul-Hak
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Abstract
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Arylsulphatases B and Bm (arylsulphate sulphohydrolase; E.C. 3.1.6.1) from rat uterus were purified and characterized. Arylsulphatases B and Bm were purified 286-fold and 112-fold with an overall recovery 23% and 5.4% respectively. On disc gel electrophoresis, both final preparations of arylsulphatases B and Bm showed one protein band. These enzymes showed normal time-activity relationship with p-nitrocatechol sulphate as substrate. The K_m and V_(max) values were 2.0×10^(-3) M and 20.8 nmol/min for arylsulphatase B and 3.9×10^(-3) M and 67 nmol/min for arylsulphatase Bm, respectively. Rat uterus contained significant quantities (16∼20% of total arylsulphatase) of an anionic form of arylsulphatase B (arylsulphatase Bm). The physico-chemical properties of arylsulphatase Bm were very similar to those of arylsulphatase B with respect to pH optimum, heat stability, the types of inhibition by sulphate, sulphite and phosphate ions, molecular weight, temperature optimum, and time-activity relationship.
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