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dc.contributor.authorCavada, B. S.-
dc.contributor.authorBari, Alfa Umaro-
dc.contributor.authorPinto-Junior, Vanir Reis-
dc.contributor.authorLóssio, Cláudia Figueiredo-
dc.contributor.authorSilva, Mayara Torquato Lima da-
dc.contributor.authorSouza, Luis Augusto Gomes-
dc.contributor.authorOliveira, Messias Vital-
dc.contributor.authorSouza-Filho, Claudio Henrique Dahne-
dc.contributor.authorCorreia, Sarah Elizabeth Gomes-
dc.contributor.authorVital, Ana Paula Moreira Sousa-
dc.contributor.authorLima, Lara Dias-
dc.contributor.authorOsterne, Vinicius José Silva-
dc.contributor.authorNascimento, K. S.-
dc.date.accessioned2020-06-15T21:35:07Z-
dc.date.available2020-06-15T21:35:07Z-
dc.date.issued2020-
dc.identifier.urihttps://repositorio.inpa.gov.br/handle/1/16516-
dc.description.abstractLectins 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.en
dc.language.isoenpt_BR
dc.relation.ispartofVolume 145, Pags. 845-855pt_BR
dc.rightsRestrito*
dc.subjectSodium Dodecyl Sulfateen
dc.subjectLectinen
dc.subjectMannoseen
dc.subjectSepharoseen
dc.subjectAmino Acid Sequenceen
dc.subjectAntiinflammatory Activityen
dc.subjectAnti-microbial Activityen
dc.subjectAntinociceptionen
dc.subjectArtemiaen
dc.subjectArtemia Naupliien
dc.subjectBiological Activityen
dc.subjectBrasilen
dc.subjectControlled Studyen
dc.subjectDrug Analysisen
dc.subjectDrug Protein Bindingen
dc.subjectDrug Purificationen
dc.subjectDrug Screeningen
dc.subjectIon Exchange Chromatographyen
dc.subjectLc50en
dc.subjectLegumeen
dc.subjectMass Spectrometryen
dc.subjectMinimum Inhibitory Concentrationen
dc.subjectMolecular Weighten
dc.subjectNonhumanen
dc.subjectParkia Biglobosaen
dc.subjectParkia Panurensisen
dc.subjectParkia Platycephalaen
dc.subjectPhen
dc.subjectSeed Planten
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectTemperatureen
dc.titlePurification 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 effectsen
dc.typeArtigopt_BR
dc.identifier.doi10.1016/j.ijbiomac.2019.10.102-
dc.publisher.journalInternational Journal of Biological Macromoleculespt_BR
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