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

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Abstract:

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.





Keywords: Glycine max; Korean large black soybean; biological properties; lectin; purification; seeds

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986610791190309

Publication date: June 1, 2010

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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