Biochemical and Functional Properties of a Lectin Purified from Korean Large Black Soybeans — A Cultivar of Glycine Max

Lectins, a class of proteins that reversibly and non-enzymatically bind specific sugars, have been purified from different kinds of legumes. In this study, a 48-kDa lectin (KBL) was purified from Korean large black soybeans using liquid chromatography. The specific hemagglutinating activity of the KBL was 4096 titer/mg. EDTA-induced loss of hemagglutinating activity of KBL could be recovered by addition of Fe3+ ions and some divalent cations as Ca2+, Mn2+, Fe2+, Cu2+, Zn2+, and Pb2+. Sugars such as D-(+)-galactose, D-(+)-raffinose, L-(+)-arabinose, α-D-(+)-melibiose, and α-lactose could inhibit the hemagglutinating activity of the lectin. Furthermore, the protein showed high thermal stability as well as stability over a wide range of pH values. KBL inhibited HIV-1 reverse transcriptase activity with an IC50 of 1.38 μM. However, it was destitute of cytokine releasing, mitogenic, ribonuclease and antifungal activities. In addition, inhibitory activity toward nasopharyngeal cell lines was undetectable in KBL at concentrations up to 20 μM.