10.6084/m9.figshare.5644996.v1
ANTÔNIA S. DE OLIVEIRA
ANTÔNIA S. DE
OLIVEIRA
CLÁUDIA F. LÓSSIO
CLÁUDIA F.
LÓSSIO
ANNE J. RANGEL
ANNE J.
RANGEL
MARIA G.Q. MARTINS
MARIA G.Q.
MARTINS
FERNANDO E.P. DO NASCIMENTO
FERNANDO E.P. DO
NASCIMENTO
MARIA L.L. DE ANDRADE
MARIA L.L. DE
ANDRADE
BENILDO S. CAVADA
BENILDO S.
CAVADA
SÍRLEIS R. LACERDA
SÍRLEIS R.
LACERDA
KYRIA S. DO NASCIMENTO
KYRIA S. DO
NASCIMENTO
Detection, purification and characterization of a lectin from freshwater green algae Spirogyra spp.
SciELO journals
2017
algae
characterization
lectin
purification
2017-11-29 12:35:48
Dataset
https://scielo.figshare.com/articles/dataset/Detection_purification_and_characterization_of_a_lectin_from_freshwater_green_algae_Spirogyra_spp_/5644996
<div><p>ABSTRACT Freshwater algae are rich sources of structurally biologically active metabolites, such as fatty acids, steroids, carotenoids and polysaccharides. Among these metabolites, lectins stand out. Lectins are proteins or glycoproteins of non-immune origin which bind to carbohydrates or glycoconjugates, without changing ligand structure. Many studies have reported on the use of Spirogyra spp. as effective bioindicators of heavy metals; however, reports on Spirogyra molecular bioprospecting are quite limited. Therefore, this study aimed to detect, isolate, purify and characterize a lectin present in the freshwater green algae Spirogyra. Presence of the lectin protein in the extract was detected by hemagglutination assays. Subsequently, the protein extract was subjected to a sugar inhibition assay to identify the lectin-specific carbohydrate. Following this, the extract was applied to a guar gum column to afford the pure lectin. The lectin was inhibited by N-acetyl-glucosamine and N-acetyl-beta-D-mannose, but more strongly by D-galactose. The apparent molecular mass of the purified lectin was evaluated by Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). Electrophoretic analysis revealed a single protein band with an apparent molecular mass of 56 kDa. Thus, it could be concluded that a lectin was purified from Spirogyra spp.</p></div>