아릴설파타아제 A를 쥐의 뇌로부터 분리하여 $(NH_4)_2SO_4$침전, DEAE-셀룰로즈, Con A-Sepharose 4B 크로마토크래피 및 Sephadex G-200 젤 여과법으로 7%의 회수율로 90배 정제하였다. 기질로서 p-nitrocatechol sulfate를 사용하였을 때 정제된 아릴설파타아제 A의 활성도는 $6.8;{mu}mole/min/mg$ protein이였으며, $K_m$과 $V_{max}$값은 각각 0.6 mM과 $7.1;{mu}mole/min/mg$ protein이었다. 효소 활성의 최적 pH는 pH 5.2와 5.8이며 아릴설파타아제 A의 분자량은 젤 여과법으로 pH 7.4에서 120,000으로 나타났다. 아릴설파타아제 A는 pH 4.5에서 두 분자가 결합하여 분자량 230,000의 이합체를 형성하였다. 이 효소의 촉매에 참여하는 group를 밝히기 위해 각종 단백질 개조용 시약들을 검토했다. 이둘중 phenylglyoxal, N-ethyl-maleimide, p-chloromercuribenzoate 및 1-ethyl-3(dimethylaminopropyl)carbodiimide는 효소를 효과적으로 저해시키는 것으로 관찰되었다.
Arylsulfatases A (arylsulfate sulfohydrolase, EC 3.1.6.1) from rat brain was separated and purified 90-fold with 7% recovery. The purification steps involved ammonium sulfate fractionation, DEAE-Cellulose ion exchange chromatography, concanavalin A-Sepharose 4B affinity chromatography and gel filtration on Sephadex G-200. The specific activity of arylsulfatase A with p-nitrocatechol sulfate as substrate was $6.8;{mu}mole/min/mg$ protein. Arylsulfatase A had two pH optima, pH 5.2 and 5.8, and the molecular weight of the enzyme was estimated to 120,000 by gel filtration on Sephadex G-200 at pH 7.4. The arylsulfatase A undergoes self-associati on to dimeric form with molecular weight of 230,000 at pH 4.5. In order to verify the catalytic groups of arylsulfatase A, the effects of the various chemical reagents for protein modification were tested. It was observed that the enzyme was inactivated by phenylglyoxal, N-ethylmaleimide, p-chloromercuribenzoate, and 1-ethyl-3(dimethylaminopropyl)carbodiimide.
