Publikation: Isolation by ConA binding of haustoria from different rust fungi and comparison of their surface qualities
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Rust haustoria isolated from infected leaf tissue strongly bind to ConA. This property was exploited to purify them by affinity chromatography on a ConA-Sepharose macrobead column. Haustoria were obtained with more than 90% purity and yields of up to 50%. Binding of haustoria to the column was partially inhibited by a ConA-specific sugar, methyl ct-D-mannopyranoside. Compared to ConA, Lens culinaris agglutinin and wheat germ agghitinin were less efficient affinity ligands. Using ConA-Sepharose, rust haustoria from a variety of sources could be isolated with equal efficiency, indicating that they have similar carbohydrate surface properties. The haustoria maintained their typical shape after the isolation procedure, which suggests a rather rigid wall structure. The morphology of haustoria was characteristic both for a given species and the nuclear condition of the rust mycelium. Electron microscopy of isolated haustoria revealed an intact haustorial wall surrounded by a fibrillar layer presumably derived from the extrahaustorial matrix. The matrix thus appears to represent a layer with geMike properties which is rich in ConA-binding carbohydrates and connected to the haustorial wall but not to the host-derived extrahaustorial membrane.
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HAHN, Matthias, Kurt MENDGEN, 1992. Isolation by ConA binding of haustoria from different rust fungi and comparison of their surface qualities. In: Protoplasma. 1992, 170(3-4), pp. 95-103. ISSN 0033-183X. eISSN 1615-6102. Available under: doi: 10.1007/BF01378785BibTex
@article{Hahn1992Isola-6657,
year={1992},
doi={10.1007/BF01378785},
title={Isolation by ConA binding of haustoria from different rust fungi and comparison of their surface qualities},
number={3-4},
volume={170},
issn={0033-183X},
journal={Protoplasma},
pages={95--103},
author={Hahn, Matthias and Mendgen, Kurt}
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<dcterms:abstract xml:lang="eng">Rust haustoria isolated from infected leaf tissue strongly bind to ConA. This property was exploited to purify them by affinity chromatography on a ConA-Sepharose macrobead column. Haustoria were obtained with more than 90% purity and yields of up to 50%. Binding of haustoria to the column was partially inhibited by a ConA-specific sugar, methyl ct-D-mannopyranoside. Compared to ConA, Lens culinaris agglutinin and wheat germ agghitinin were less efficient affinity ligands. Using ConA-Sepharose, rust haustoria from a variety of sources could be isolated with equal efficiency, indicating that they have similar carbohydrate surface properties. The haustoria maintained their typical shape after the isolation procedure, which suggests a rather rigid wall structure. The morphology of haustoria was characteristic both for a given species and the nuclear condition of the rust mycelium. Electron microscopy of isolated haustoria revealed an intact haustorial wall surrounded by a fibrillar layer presumably derived from the extrahaustorial matrix. The matrix thus appears to represent a layer with geMike properties which is rich in ConA-binding carbohydrates and connected to the haustorial wall but not to the host-derived extrahaustorial membrane.</dcterms:abstract>
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