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丝状指形线虫亲和纯化排泄分泌蛋白酶的部分特性分析

Partial characterization of affinity purified excretory-secretory protease from Setaria digitata.

作者信息

Murugan A, Raj R K

机构信息

Department of Biochemistry, University of Kerala, Kariavattom, Thiruvananthapuram, India.

出版信息

Indian J Exp Biol. 1997 May;35(5):538-40.

PMID:9378523
Abstract

Excretory-secretory protease of S. digitata released along with the microfilariae (mf) during hatching has been purified by affinity chromatography. No other activity could be detected in the affinity purified material. Homogeneity is checked by native PAGE. It has a pH optimum of 5.4 and a molecular weight of 70 kD. The purified material showed positivity against antibodies raised against ES material.

摘要

通过亲和层析法纯化了指状丝虫在微丝蚴孵化过程中释放的排泄-分泌蛋白酶。在亲和纯化的物质中未检测到其他活性。通过非变性聚丙烯酰胺凝胶电泳检查其纯度。其最适pH为5.4,分子量为70kD。纯化后的物质对针对排泄-分泌物质产生的抗体呈阳性反应。

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