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DC Field | Value | Language |
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dc.contributor.author | Cavada, Benildo S. | - |
dc.contributor.author | Santos, Cláudia F. | - |
dc.contributor.author | Grangeiro, Thalles B. | - |
dc.contributor.author | Nunes, Edson P. | - |
dc.contributor.author | Sales, Patricia V. P. | - |
dc.contributor.author | Ramos, Ronaldo L. | - |
dc.contributor.author | Sousa, Flávia A. M. de | - |
dc.contributor.author | Crisostomo, Clebia V. | - |
dc.contributor.author | Calvete, Juan J. | - |
dc.date.accessioned | 2022-03-04T16:46:15Z | - |
dc.date.available | 2022-03-04T16:46:15Z | - |
dc.date.issued | 1998 | - |
dc.identifier.citation | CAVADA, Benildo S. et al. Purification and characterization of a lectin from seeds of Vatairea macrocarpa Duke. Phytochemistry, [s. l.], v. 49, n. 3, p. 675-680, 1998. | pt_BR |
dc.identifier.uri | http://www.repositorio.ufc.br/handle/riufc/64278 | - |
dc.description.abstract | The protein, a galactose binding lectin made up of a misture of full length chains and endogenous C- and N-terminal fragments, was purified from Vatairea macrocarpa seeds and its properties were studied. A lectin from Vatairea macrocarpa Duke seeds (VML) was isolated using affinity chromatography on a guar gum column. The lectin, a glycoprotein without erythrocyte specificity, displays specificity to galactose and some derivatives. On SDS-polyacrylamide gels, V. macrocarpa seed lectin is composed of two major high-Mr bands of 34 and 32 kDa and two minor low-Mr bands of 22 and 13 kDa. N-Terminal sequencing showed that the 34, 32, and 13 kDa products possess identical N-terminal sequence, which display best similarity with the N-terminal portion of Robinia pseudoacacia lectins (RPL). On the other hand, the N-terminal sequence of the 22 kDa band can be aligned with an internal sequence of RPL starting at residue 149 of the cDNA-derived sequence. These data indicate that, like other leguminous lectins, VML is made up of a mixture of onechain 30–35 kDa glycoforms and of 22 and 13 kDa endogenous C- and N-terminal fragments. Size-exclusion chromatography indicated that, at neutral pH, VML is predominantly a dimeric (70 kDa) protein, although tetramers (115 kDa) and larger aggregates (300 kDa) were also present. | pt_BR |
dc.language.iso | pt_BR | pt_BR |
dc.publisher | Phytochemistry | pt_BR |
dc.rights | Acesso Aberto | pt_BR |
dc.subject | Vatairea macrocarpa | pt_BR |
dc.subject | Leguminosae | pt_BR |
dc.subject | Lectin | pt_BR |
dc.subject | Affinity chromatography | pt_BR |
dc.subject | D-galactose-binding | pt_BR |
dc.subject | Amino acid sequence | pt_BR |
dc.title | Purification and characterization of a lectin from seeds of Vatairea macrocarpa Duke | pt_BR |
dc.type | Artigo de Periódico | pt_BR |
Appears in Collections: | DBIO - Artigos publicados em revista científica |
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File | Description | Size | Format | |
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1998_art_bscavada.pdf | 4,62 MB | Adobe PDF | View/Open |
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