Immunoaffinity Purification of the Class V Chitin Synthase of Wangiella (Exophiala) dermatitidis

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 te...

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Bibliographic Details
Published in:Preparative biochemistry & biotechnology 2009-01, Vol.39 (3), p.277-288
Main Authors: Abramczyk, Dariusz, Szaniszlo, Paul J.
Format: Article
Language:English
Subjects:
Black pathogenic fungus
Blotting, Western
Catalytic Domain
Chitin synthase
Chitin Synthase - chemistry
Chitin Synthase - isolation & purification
Chromatography, Affinity - methods
Electrophoresis, Polyacrylamide Gel
Exophiala - enzymology
Exophiala dermatitidis
Immunoaffinity purification
Transmembrane protein
Wangiella
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Summary: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.
ISSN:1082-6068
1532-2297
DOI:10.1080/10826060902953244