| Autor: |
Francisco Nascimento, Pereira-Junior, Helton Colares, Silva, Beatriz Tupinambá, Freitas, Bruno Anderson Matias, Rocha, Kyria Santiago, Nascimento, Celso Shinitti, Nagano, Rodrigo Bainy, Leal, Alexandre Holanda, Sampaio, Benildo Sousa, Cavada |
| Rok vydání: |
2012 |
| Předmět: |
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| Zdroj: |
Journal of molecular recognition : JMR. 25(8) |
| ISSN: |
1099-1352 |
| Popis: |
Platymiscium floribundum lectin (PFL), a mannose/N-acetyl-D-glucosamine-specific lectin, was isolated from P. floribundum seeds using Sepharose-mannose affinity media chromatography. PFL is a glycoprotein that is a potent agglutinin for rabbit erythrocytes. In addition, PFL is highly stable because it is able to maintain its hemagglutinating activity after exposure to temperatures of up to 60 °C for 1 h and exposure to a wide pH range. The PFL purification process was monitored using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the results showed that the purified lectin consists of a single band with a molecular mass of approximately 29 kDa in either the presence or the absence of a reducing agent. The analysis of purified PFL by electrospray ionization-mass spectrometry showed that most ions had a molecular weight of 27,053 ± 2 Da, and other less abundant ions had similar molecular weights. Gel filtration shows that the lectin exists as a dimer in solution with mass at approximately 65 kDa. Sixteen peptides were sequenced, and as a result, a total of 130 amino acids were identified and resulted in a coverage of approximately 65% of the PFL sequence. The partial sequence of PFL was aligned with sequences of other lectins from evolutionarily related species, and PFL showed considerable similarity to the other lectins. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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