Isolation and Purification of Lection from Momordica balsamina Seeds
Mariam Abbas Ibrahim, Bakri Osman Saeed, Emadeldin Hassan ElsaidKonozy, Samia Mahdi Ahmed, MakarimElfadil Mohamed

Abstract

Background: Lectins are multivalent proteins of non-immune origin that reversibly and non-enzymatically bind carbohydrates with high specificity for the chemical structure of the glycan array without changing their structure. Lectins have been mostly isolated from plant seeds although recently it had been known to be found in other plant tissues, prokaryotes and higher animals.

Objectives: The present study aimed to isolate and purify Momordica balsamina seedslectin (MbSL). Materials and methods: A season fresh of Momordica balsamina fruit seeds were brought from urban areas of Sudan (Gadrif and north Kurdofan states), then the lectin was isolated from saline extract by affinity chromatography on alpha agarose lactose matrix.

Results: The lectin content was about 1200 mg/ 100 g dry flour.MbSL agglutinated all human RBCs type with preference toward the O blood group. The lectin also agglutinated mouse, donkey and cow blood cells and showed no effect on gout erythrocytes. Lactose was the most potent inhibitor of MbSLhemagglutinating activity, (minimal inhibitory concentration) MIC = 25mM, followed by galactose, MIC=50 mM, and then arabinose, MIC= 100mM.

Conclusion: a lactose-binding lectin from seeds of Momordica balsamina medicinal plant shares a high degree of similarity with other Cucurbitaceae family lectins in term of their sugar specificity.