Purification, Chemical, and Immunochemical Properties of a New Lectin fromMimosoideae (Parkia Discolor)
| Autor: | Thalles B. Grangeiro, Luis A. G. Souza, Dantas Ar, Márcio V. Ramos, K B Leite, Benildo Sousa Cavada, V.P.T. Pinto, Bomfim Lr, Juan J. Calvete, Beatriz Tupinamba Freitas, Madeira Svf, Lopes Mc |
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| Rok vydání: | 2000 |
| Předmět: |
Glycan
Mannose Biochemistry Chromatography Affinity chemistry.chemical_compound Affinity chromatography Lectins Animals Amino Acids Glycoproteins Plants Medicinal biology Molecular mass Lectin Fabaceae Hemagglutination Tests General Medicine Hemagglutination Inhibition Tests biology.organism_classification Molecular Weight chemistry Concanavalin A biology.protein Electrophoresis Polyacrylamide Gel Parkia Rabbits Mimosoideae Plant Lectins Biotechnology |
| Zdroj: | Preparative Biochemistry and Biotechnology. 30:271-280 |
| ISSN: | 1532-2297 1082-6068 |
| DOI: | 10.1080/10826060008544966 |
| Popis: | A glucose/mannose-binding lectin was isolated from seeds of Parkia discolor (Mimosoideae) using affinity chromatography on Sephadex G-100 gel. The protein presented a unique component in SDS-PAGE corresponding to a molecular mass of 58,000 Da, which is very similar to that of a closely related lectin from Parkia platycephala. Among the simple sugars tested, mannose was the best inhibitor, but biantennary glycans, containing the trimannoside core, present in N-glycoproteins, also seem to be powerful inhibitors of the haemagglutinating activity induced by the purified lectin. The protein was characterised by high content of glycine and proline and absence of cysteine. Rabbit antibodies, anti-P. platycephala seed lectin, recognised the P. discolor lectin. However, no cross-reaction was observed when a set of other legume lectins from sub-family Papilionoideae and others from families Moraceae and Euphorbiaceae were assayed with the Parkia lectins. This suggests that Parkia lectins comprise a new group of legume lectins exhibiting distinct characteristics. |
| Databáze: | OpenAIRE |
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