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.

Autor: Cavada BS; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil. Electronic address: bscavada@ufc.br., Bari AU; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Pinto-Junior VR; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Lossio CF; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Silva MTL; Laboratório de Neuroquímica 3 - Transdução de Sinal no SNC, Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Souza LAG; Instituto Nacional de Pesquisas da Amazônia-INPA, Manaus, Amazonas, Brazil., Oliveira MV; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Souza-Filho CHD; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Correia SEG; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Vital APMS; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Lima LD; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Osterne VJS; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil., Nascimento KS; Laboratório de Moléculas Biologicamente Ativas (BioMol-Lab), Universidade Federal do Ceará (UFC), Fortaleza, Ceará, Brazil.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2020 Feb 15; Vol. 145, pp. 845-855. Date of Electronic Publication: 2019 Nov 15.
DOI: 10.1016/j.ijbiomac.2019.10.102
Abstrakt: 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 LC 50 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.
(Copyright © 2019 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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