Purification and partial characterization of two lectins from Momordica charantia.

2 different lectins have been purified from the seeds of Momordica charantia by gel-filtration and ion-exchange chromatography. These 2 lectins appear to be composed of 2 subunits of 26,000 daltons. Protein fraction I, but not II, showed agglutinating activity toward human type-O red blood cells. The amino acid compositions and amino-terminal sequences of these two homologous proteins are quite different.