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从大鼠肝脏中纯化溶酶体芳基硫酸酯酶B及其在亲和免疫电泳中与凝集素的反应性。

Purification of lysosomal arylsulfatase B from rat liver and its reactivity with lectins in affinity immunoelectrophoresis.

作者信息

Wójczyk B S, Hoja D A, Lityńska A M

机构信息

Department of Animal Physiology, Jagiellonian University, Kraków, Poland.

出版信息

Int J Biochem. 1992 Oct;24(10):1561-71. doi: 10.1016/0020-711x(92)90172-w.

Abstract
  1. Arylsulfatase B (ASB) from lysosomal fraction of rat liver were isolated and purified 260-fold with a recovery of about 5%. 2. The enzyme in gradient PAGE 4-30% followed by immunoelectrophoresis migrated as a single peak of M(r) 84,000. The pI, measured by isoelectrofocusing in agarose followed by immunoelectrophoresis, was equal to 6.7. 3. ASB reacted with Con A, LCA, PSA, LTL, WGA, RCAI and did not react with PHA, SBA, HPA, CAA and PAL in crossed affino-immunoelectrophoresis or rocket immunoelectrophoresis. These results permit of preliminary elucidation of ASB glycan structure.
摘要
  1. 从大鼠肝脏溶酶体部分分离并纯化了芳基硫酸酯酶B(ASB),纯化了260倍,回收率约为5%。2. 该酶在4 - 30%梯度聚丙烯酰胺凝胶电泳(PAGE)后进行免疫电泳,迁移为单一峰,相对分子质量(M(r))为84,000。通过在琼脂糖中进行等电聚焦后再进行免疫电泳测定的等电点(pI)为6.7。3. 在交叉亲和免疫电泳或火箭免疫电泳中,ASB与刀豆球蛋白A(Con A)、扁豆凝集素(LCA)、花生凝集素(PSA)、荆豆凝集素(LTL)、麦胚凝集素(WGA)、蓖麻凝集素I(RCAI)反应,而不与植物血凝素(PHA)、大豆凝集素(SBA)、辣根过氧化物酶(HPA)、鸡冠花凝集素(CAA)和菜豆凝集素(PAL)反应。这些结果有助于初步阐明ASB聚糖结构。

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