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大肠杆菌108(pPAHD1)青霉素G酰化酶的纯化与结晶

Purification and Crystalline of Penicillin G Acylase
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摘要 大肠杆菌108(pPAHD1)发酵液经离心沉淀,蔗糖高渗处理得到青霉素酰化酶粗品,再经苯乙酰胺-Sepharose4B疏水层析和DEAE-Cellulose DE-52分离纯化,得到可用于结晶的青霉素G酰化酶。在55%饱和度硫酸铵-0.05mol/LPBS,pH7.5条件下批量静置得到该酶晶体。 The crude penicillin G acylase were extracted from E.coli 108 cells by centrifuged and treated with high osmotic shock . Further purified by hydrophobic interaction chromatography with Phenylacetamide-Sepharose 4B and DEAE-Cellulose DE52. After that we got a high purity penillin G acylase to crystallize .Using bath method the crystals of the enzyme were grown from 55% saturated ammonium sulfate in 0.05 mol / L phosphate buffer, pH7.5
出处 《河北大学学报(自然科学版)》 CAS 1992年第3期57-61,共5页 Journal of Hebei University(Natural Science Edition)
关键词 纯化 青霉素酰化酶 大肠杆菌108 Penicillin G Acylase , Purification, Crystalline.
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参考文献4

  • 1王立,李洲,黄丽华.615近交系小鼠血红蛋白遗传学分析[J]动物学报,1986(03).
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  • 4Pramod B. Mahajan,Prabhakar S. Borkar. Novel approaches to the purification of penicillin acylase[J] 1984,Applied Biochemistry and Biotechnology(5-6):421~437

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