Biochemical and functional properties of a lectin purified from the seeds of Cicer arietinum L.

Abstract

A 35kDa rabbit erythrocyte agglutinating lectin from the seeds of Cicer arietinum was purified and designated as CAL. The lectin was inhibited by fetuin and N-acetyl-d-galactosamine at a concentration of 20 and 50mM respectively, but not by simple mono or oligosaccharides. CAL is active between pH 5 and 10 presented thermo stability up to 50°C and demonstrated DNA damage inhibition at 30µg concentration. The lectin elicited maximum mitogenic activity towards mice splenocytes at 7.5µg ml- 1. CAL exerted an inhibitory activity on HIV-1 reverse transcriptase with IC50 of 180µM. CAL abilities in animal bioassay resulted decreased levels of total triglyceride and creatinine. In vitro and in vivo studies revealed that CAL may constitute an important role impending biomedical applications.