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

Mimosoideae Parkia biglobosa Molecular mass
DOI: 10.1016/j.ijbiomac.2019.10.102 Publication Date: 2019-11-15T16:57:50Z
ABSTRACT
Lectins are proteins that have as one of their main characteristics recognizing and reversibly binding to carbohydrates. In this work, it was possible purify characterize a lectin from Parkia panurensis (Leguminosae family; Mimosoideae subfamily) seeds by combination the techniques: protein precipitation, along with affinity then ion exchange chromatography using Sepharose-mannose diethylaminoethyl matrices, respectively. The pure lectin, called PpaL, has D-mannose, D-glucose derivatives. PpaL stable over wide range temperature pH, showed an SDS-PAGE profile only band apparent mass 45 kDa, subsequently confirmed spectrometry, presented molecular 50,566 ± 1 Da. PAGE analysis exclusion demonstrated is dimer in solution. Partial sequencing primary structure resulted total 334 amino acid residues approximately 97% similarity biglobosa platycephala seed lectins. shown be toxic against Artemia nauplii had LC50 20 µg/mL. effects biological activities these make them important biotechnological tools, demonstrating importance bioprospection new
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (35)
CITATIONS (15)