Proteins that can agglutinate red blood cells with known sugar specificity and have ability to bind carbohydrates are referred to as Lectins. The legume lectins were also found to have hemagglutinating properties because of their ability to bind glycans on the cell surface. The abundance of these proteins in the soluble extracts of legume seeds (up to ∼5%–10% total protein) enabled many lectins to be isolated and characterized. This study showed the existence and variability in agglutinating characters when the extracts of the leaves and seeds of Lablab purpureus were subjected to blood groups O and B. Protein estimation and hemagglutinating activities of the Lectin content in Lablab extracts against the human blood group used showed that accession TLn 7 and TLn 13 showed low Lectin and high protein. Accession TLn7 showed promising diversity of agronomic attributes, the low lectin in both seeds and leaves and exhibited a high concentration of protein in the seeds. Of all the accessions of Lablab beans evaluated in this study, accessions TLn12, TLn13, TLn36, TLn45, TLn46, TLn57 and TLn70 showed great potential in their morphological traits and biochemical components. The lectins activity greatly varied between the seeds and leaves of the accessions investigated, despite belonging to the same species. There was an existence of genetic induced variability in the Protein estimation and hemagglutinating activities of the Lectin content in extracts of the Lablab accessions considered against the human blood groups O and B. Therefore, genetic compatibility study is required among these accessions and most importantly with other cultivars from other developed countries.