| Autor: |
Rômulo Farias, Carneiro, Arthur Alves, de Melo, Fernando Edson Pessoa do, Nascimento, Clareane Avelino, Simplicio, Kyria Santiago do, Nascimento, Bruno Anderson Matias da, Rocha, Silvana, Saker-Sampaio, Raniere da Mata, Moura, Sula Salani, Mota, Benildo Sousa, Cavada, Celso Shiniti, Nagano, Alexandre Holanda, Sampaio |
| Rok vydání: |
2012 |
| Předmět: |
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| Zdroj: |
Journal of molecular recognition : JMR. 26(1) |
| ISSN: |
1099-1352 |
| Popis: |
Two new lectins named Halilectin 1 (H-1) and Halilectin 2 (H-2) were isolated from the marine sponge Haliclona caerulea using a combination of affinity chromatography on stroma fixed onto Sephadex G-25 and cation and anion exchange chromatography. H-1 is a monomeric protein with a molecular mass of 40 kDa estimated using sodium dodecyl sulfate polyacrylamide gel electrophoresis and 15 kDa estimated using a TSK gel. Conversely, H-2 is a homodimeric protein with 15 kDa monomers linked via weak interactions. H-1 more effectively agglutinates trypsinized rabbit erythrocytes, whereas H-2 more effectively agglutinates native rabbit erythrocytes. The hemagglutinating activity of H-1 could be not inhibited by any tested sugars, but H-2 was inhibited by orosomucoid and porcine stomach mucin. Neither lectin was dependent on divalent ions. H-1 was stable at basic pH range and temperatures up to 50 °C, whereas H-2 was stable at acid pH range and temperatures up to 80 °C. The H. caerulea lectins exhibited dose-dependent toxicity against Artemia nauplii. Additionally, 76% of the primary structure of H-2 was determined using tandem mass spectrometry to contain a unique amino acid sequence with no similarity to any members of the animal lectin family. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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