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皮炎外瓶霉(枝孢瓶霉)V类几丁质合酶的免疫亲和纯化

Immunoaffinity purification of the class V chitin synthase of Wangiella (Exophiala) dermatitidis.

作者信息

Abramczyk Dariusz, Szaniszlo Paul J

机构信息

Section of Molecular Genetics and Microbiology, School of Biological Science and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA.

出版信息

Prep Biochem Biotechnol. 2009;39(3):277-88. doi: 10.1080/10826060902953244.

Abstract

The class V chitin synthase is unique because it has a myosin motor-like domain fused to its catalytic domain. The biochemical properties of this enzyme and its function remain undefined beyond the knowledge that it is the only single chitin synthase required for sustained cell growth at elevated temperatures and, consequently, virulence. This report describes our successful efforts to isolate and purify an active and soluble form of the enzyme from the cell membranes of Wangiella by using a specific polyclonal antibody. To our knowledge, this is the first purification of a single chitin synthase of a filamentous fungus.

摘要

V类几丁质合酶很独特,因为它的催化结构域融合了一个类似肌球蛋白马达的结构域。除了知道它是高温下持续细胞生长以及毒力所需的唯一一种单一几丁质合酶外,这种酶的生化特性及其功能仍不明确。本报告描述了我们通过使用特异性多克隆抗体,成功地从弯孢霉菌细胞膜中分离并纯化出该酶的活性可溶形式。据我们所知,这是丝状真菌单一几丁质合酶的首次纯化。

相似文献

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Immunoaffinity purification of the class V chitin synthase of Wangiella (Exophiala) dermatitidis.
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