Purification and primary structure of a novel mannose-specific lectin from Centrolobium microchaete Mart seeds

International Journal of Biological Macromolecules
Mayron A VasconcelosBenildo Sousa Cavada

Abstract

This study aimed to purify and characterize a novel mannose-binding lectin from the seeds of Centrolobium microchaete. Centrolobium microchaete lectin (CML) was purified by affinity chromatography in mannose-Sepharose-4B column. CML agglutinated rabbit erythrocytes and was inhibited by D-mannose, α-methyl-D-mannoside, D-glucose, N-Acetyl-D-glucosamine and sucrose. The lectin was stable at pH 7.0 and 8.0 and temperatures up to 60°C. The monomeric form of CML showed approximately 28kDa, and its native form is probably a homodimer, as determined by gel filtration chromatography. The primary structure of CML was determined by tandem mass spectrometry that showed CML as a protein with two distinct forms (isolectins CML-1 and CML-2) with 246 and 247 residues, respectively. CML-2 possesses one residue of Asn more than CML-1 in C-terminal. The primary structure of CML agrees with the molecular weights found by electrospray ionization mass spectrometry: 27,224 and 27,338Da for CML-1 and CML-2, respectively. CML is a metal-dependent glycoprotein. Moreover, the glycan composition of CML and its structure were predicted.

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Citations

Mar 8, 2016·Archives of Biochemistry and Biophysics·Alysson Chaves AlmeidaBenildo Sousa Cavada
Jan 13, 2019·International Journal of Molecular Sciences·Annick BarrePierre Rougé
Dec 21, 2019·International Journal of Biological Macromolecules·Kyria Santiago NascimentoBenildo Sousa Cavada
Sep 5, 2017·International Journal of Biological Macromolecules·Benildo Sousa CavadaKyria Santiago Nascimento
May 29, 2018·International Journal of Biological Macromolecules·Antonio Hadson Bastos NecoBenildo Sousa Cavada
Nov 24, 2021·Natural Product Research·Luiz Gonzaga do Nascimento NetoEdson Holanda Teixeira

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