Open AccessPurification of melibiose‐binding lectins from two cultivars of Chinese black soybeans
Author(s) -
Lin Peng,
Ye Xiujuan,
Ng TB
Publication year - 2008
Publication title -
acta biochimica et biophysica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.771
H-Index - 57
eISSN - 1745-7270
pISSN - 1672-9145
DOI - 10.1111/j.1745-7270.2008.00488.x
Subject(s) - lectin , melibiose , soybean agglutinin , size exclusion chromatography , biochemistry , thermostability , sepharose , glycine , molecular mass , chemistry , biology , enzyme , amino acid , agglutinin , maltose
A dimeric 50 kDa melibiose‐binding lectin was isolated from the seeds of the cultivar of soybean ( Glycine max ), called the small glossy black soybean. The isolation procedure comprised ion exchange chromatography on Q Sepharose, SP Sepharose and Mono Q followed by gel filtration on Superdex 75. The lectin was adsorbed on all three ion exchangers, and it exhibited an N‐terminal sequence identical to that of soybean lectin. Of all the sugars tested, melibiose most potently inhibited the hemagglutinating activity of the lectin, which was stable between pH 3‐12 and 0‐70 °C. The lectin evoked maximal mitogenic response at about the same molar concentration as Con A. However, the response was much weaker. The soybean lectin inhibited the activity of HIV‐1 reverse transcriptase as well as the proliferation of breast cancer MCF7 cells and hepatoma HepG2 cells with an IC 50 of 2.82 μM, 2.6 μM and 4.1 μM, respectively. There was no antifungal activity. Another lectin was isolated from a different cultivar of soybean called little black soybean. The lectin was essentially similar to small glossy black soybean lectin except for a larger subunit molecular mass (31 kDa), a more potent mitogenic activity and lower thermostability. The results indicate that different cultivars of soybean produce lectins that are not identical in every aspect.