Purification and characterization of an asialofetuin specific lectin from the rhizome of Xanthosoma violaceum Schott

Oinam Sangita Devi; Senjam Sunil Singh; K Rana; Sorokhaibam Jibankumar Singh; Wayenbam Sobhachandra Singh

doi:10.1016/j.pep.2023.106357

Purification and characterization of an asialofetuin specific lectin from the rhizome of Xanthosoma violaceum Schott

Protein Expr Purif. 2024 Jan:213:106357. doi: 10.1016/j.pep.2023.106357. Epub 2023 Aug 29.

Authors

Oinam Sangita Devi¹, Senjam Sunil Singh², K Rana¹, Sorokhaibam Jibankumar Singh¹, Wayenbam Sobhachandra Singh¹

Affiliations

¹ Laboratory of Protein Biochemistry, Biochemistry Department, Manipur University, Canchipur, Imphal, 795003, India.
² Laboratory of Protein Biochemistry, Biochemistry Department, Manipur University, Canchipur, Imphal, 795003, India. Electronic address: sunil_senjam@rediffmail.com.

PMID: 37652391
DOI: 10.1016/j.pep.2023.106357

Abstract

Lectins are proteins or glycoproteins that bind specifically and reversibly to the carbohydrate or glycoconjugates. A new lectin is purified from the rhizome of Xanthosoma violaceum Schott. by successive steps of ammonium sulfate fractionation and affinity chromatography with asialofetuin as ligand. The purified lectin was found to be a homotetramer of approximately 49 kDa with a subunit molecular weight of 12 kDa linked by non-covalent bonds. Characterization of the lectin shows that the hemagglutination activity is inhibited by asialofetuin and d-galacturonic acid. Hemagglutination activity is shown only in rabbit RBC but not in the human RBC of all blood groups. It is a metal ion-independent glycoprotein of 1.87% carbohydrate content, stable upto 40 °C and pH from 5.5 to 9. The lectin shows its optimum hemagglutination activity at 0 °C-40 °C and pH 6 to 8.5. From LC-MS/MS analysis it is confirmed that the purified lectin was not purified and characterized earlier.

Keywords: Affinity chromatography; Ammonium sulfate fractionation; Asialofetuin; Glycoprotein; Hemagglutination; Lectin.