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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Cavada BS,Bari AU,Pinto-Junior VR,Lossio CF,Silva MTL,Souza LAG,Oliveira MV,Souza-Filho CHD,Correia SEG,Vital APMS,Lima LD,Osterne VJS,Nascimento KSdoi
10.1016/j.ijbiomac.2019.10.102subject
Has Abstractpub_date
2020-02-15 00:00:00pages
845-855eissn
0141-8130issn
1879-0003pii
S0141-8130(19)37771-2journal_volume
145pub_type
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