Legumin- and vicilin-like proteins from spores of the fern Matteuccia struthiopteris
Legumin- and vicilin-like proteins have been isolated from spores of the fern Matteuccia struthiopteris. Their relationship with seed legumin and vicilin was demonstrated by cross-reactivities of antibodies directed against respective storage globulins from Vicia faba as evidenced by Western blottin...
| Veröffentlicht in: | Journal of plant physiology. - 1979. - 160(2003), 6 vom: 09. Juni, Seite 583-8 |
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| Weitere Verfasser: | , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2003
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| Zugriff auf das übergeordnete Werk: | Journal of plant physiology |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Plant Proteins Seed Storage Proteins vicilin protein, plant 9067-60-1 |
| Zusammenfassung: | Legumin- and vicilin-like proteins have been isolated from spores of the fern Matteuccia struthiopteris. Their relationship with seed legumin and vicilin was demonstrated by cross-reactivities of antibodies directed against respective storage globulins from Vicia faba as evidenced by Western blotting. The Matteuccia legumin-like protein was characterised as a 300-340 kDa holoprotein preferentially consisting of a 32 kDa alpha-chain and a 24 kDa beta-chain. Patterns of limited proteolysis of the spore legumin-like protein and seed legumins were similar as well. In contrast to seed legumins, the Matteuccia legumin-like protein is devoid of disulfide bridges between alpha- and beta-chains. A 52 kDa polypeptide of the Matteuccia vicilin-like protein, first detected by SDS gel electrophoresis, is probably encoded by a vicilin-like gene specifically expressed in Matteuccia struthiopteris spores (Shutov et al. 1998). The vicilin-like holoprotein was found to form a complex of 600 kDa apparent molecular mass, presumably composed of four vicilin-like trimers |
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| Beschreibung: | Date Completed 10.12.2003 Date Revised 13.12.2023 published: Print Citation Status MEDLINE |
| ISSN: | 1618-1328 |