Purification, Partial Characterization and Immobilization of a Mannose-Specific Lectin from Seeds of Dioclea lasiophylla Mart
Autor: | Emilio de Castro Miguel, Thaiz Batista Azevedo Rangel Miguel, Mayron Alves de Vasconcelos, Benildo Sousa Cavada, Alexandre Holanda Sampaio, Vanir Reis Pinto-Junior, Vinicius Jose Da Silva Osterne, João Batista Cajazeiras, Kyria S. Nascimento, Antônia Sâmia Fernandes do Nascimento, Mayara Queiroz Santiago, Jorge Luis Almeida Correia, Francisco N. Pereira-Junior, Celso Shiniti Nagano, Edson Holanda Teixeira |
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Jazyk: | angličtina |
Rok vydání: | 2013 |
Předmět: |
Erythrocytes
Cyanogen Pharmaceutical Science Chromatography Affinity Analytical Chemistry chemistry.chemical_compound Drug Discovery Chelating Agents chemistry.chemical_classification Plant lectins biology Sepharose Hydrogen-Ion Concentration Glycoproteomics Hemagglutinins Biochemistry Chemistry (miscellaneous) Seeds Dioclea Molecular Medicine Rabbits Protein Binding Diocleinae Ovalbumin PROTEINS lectin Dioclea lasiophylla toxicity immobilization Article Lethal Dose 50 lcsh:QD241-441 Immobilization Affinity chromatography lcsh:Organic chemistry Animals Monosaccharide Physical and Theoretical Chemistry Edetic Acid PLANT-LECTINS Chromatography Toxicity Plant Extracts Hemagglutination Protein Organic Chemistry Biology and Life Sciences Lectin Fetuin Mannose-Binding Lectins chemistry biology.protein Artemia Glycoprotein |
Zdroj: | Molecules, Vol 18, Iss 9, Pp 10857-10869 (2013) Repositório Institucional da Universidade Federal do Ceará (UFC) Universidade Federal do Ceará (UFC) instacron:UFC MOLECULES Molecules Molecules; Volume 18; Issue 9; Pages: 10857-10869 |
ISSN: | 1420-3049 |
Popis: | Lectin from the seeds of Dioclea lasiophylla (DlyL) was purified in a single step by affinity chromatography on a Sephadex (R) G-50 column. DlyL strongly agglutinated rabbit erythrocytes and was inhibited by monosaccharides (D-mannose and alpha-methyl-D-mannoside) and glycoproteins (ovalbumin and fetuin). Similar to other Diocleinae lectins, DlyL has three chains, alpha, beta and gamma, with mass of 25,569 +/- 2, 12,998 +/- 1 and 12,588 +/- 1 Da, respectively, and has no disulfide bonds. The hemagglutinating activity of DlyL was optimal in pH 8.0, stable at a temperature of 70 degrees C and decreased in EDTA solution, indicating that lectin activity is dependent on divalent metals. DlyL exhibited low toxicity on Artemia sp. nauplii, but this effect was dependent on the concentration of lectin in solution. DlyL immobilized on cyanogen bromide-activated Sepharose (R) 4B bound 0.917 mg of ovalbumin per cycle, showing the ability to become a tool for glycoproteomics studies. |
Databáze: | OpenAIRE |
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