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Title: Purification and partial characterization of a new lectin from Parkia panurensis Benth. ex H.C. Hopkins seeds (Leguminosae family; Mimosoideae subfamily) and evaluation of its biological effects
Authors: Cavada, B. S.
Bari, Alfa Umaro
Pinto-Junior, Vanir Reis
Lóssio, Cláudia Figueiredo
Silva, Mayara Torquato Lima da
Souza, Luis Augusto Gomes
Oliveira, Messias Vital
Souza-Filho, Claudio Henrique Dahne
Correia, Sarah Elizabeth Gomes
Vital, Ana Paula Moreira Sousa
Lima, Lara Dias
Osterne, Vinicius José Silva
Nascimento, K. S.
Keywords: Sodium Dodecyl Sulfate
Amino Acid Sequence
Antiinflammatory Activity
Anti-microbial Activity
Artemia Nauplii
Biological Activity
Controlled Study
Drug Analysis
Drug Protein Binding
Drug Purification
Drug Screening
Ion Exchange Chromatography
Mass Spectrometry
Minimum Inhibitory Concentration
Molecular Weight
Parkia Biglobosa
Parkia Panurensis
Parkia Platycephala
Seed Plant
Electrophoresis, Polyacrylamide Gel
Issue Date: 2020
metadata.dc.publisher.journal: International Journal of Biological Macromolecules
metadata.dc.relation.ispartof: Volume 145, Pags. 845-855
Abstract: Lectins are proteins that have as one of their main characteristics recognizing and reversibly binding to carbohydrates. In this work, it was possible to purify and characterize a lectin from Parkia panurensis (Leguminosae family; Mimosoideae subfamily) seeds by a combination of the techniques: protein precipitation, along with affinity and then ion exchange chromatography using the Sepharose-mannose and diethylaminoethyl matrices, respectively. The pure lectin, called PpaL, has affinity by D-mannose, D-glucose and derivatives. PpaL was stable over a wide range of temperature and pH, and it showed an SDS-PAGE profile of only one protein band with apparent mass of 45 kDa, subsequently confirmed by mass spectrometry, and presented a molecular mass of 50,566 ± 1 Da. PAGE analysis and molecular exclusion chromatography demonstrated that PpaL is presented as a dimer in solution. Partial sequencing of the primary structure resulted in a total of 334 amino acid residues with approximately 97% similarity to Parkia biglobosa and Parkia platycephala seed lectins. PpaL was shown to be toxic against Artemia nauplii and had an LC50 of 20 µg/mL. The effects of biological activities presented by these proteins make them important biotechnological tools, demonstrating the importance of bioprospection of new lectins. © 2019 Elsevier B.V.
metadata.dc.identifier.doi: 10.1016/j.ijbiomac.2019.10.102
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