Autor(es):
Pinto Júnior, Vanir Reis ; Santiago, Mayara Queiroz de ; Osterne, Vinícius José da Silva ; Correia, Jorge Luis Almeida ; Pereira Júnior, Francisco Nascimento ; Cajazeiras, João Batista ; Vasconcelos, Mayron Alves de ; Teixeira, Edson Holanda ; Nascimento, Antônia Sâmia Fernandes do ; Miguel, Thaiz Batista Azevedo Rangel ; Miguel, Emilio de Castro ; Sampaio, Alexandre Holanda ; Nascimento, Kyria Santiago do ; Nagano, Celso Shiniti ; Cavada, Benildo Sousa
Data: 2022
Origem: Oasisbr
Assunto(s): Dioclea lasiophylla; Diocleinae; Toxicity; Immobilization
Descrição
Lectin from the seeds of Dioclea lasiophylla (DlyL) was purified in a single step by affinity chromatography on a Sephadex® G-50 column. DlyL strongly agglutinated rabbit erythrocytes and was inhibited by monosaccharides (D-mannose and α-methyl-Dmannoside) and glycoproteins (ovalbumin and fetuin). Similar to other Diocleinae lectins, DlyL has three chains, α, β and γ, 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 °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® 4B bound 0.917 mg of ovalbumin per cycle, showing the ability to become a tool for glycoproteomics studies.
