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
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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