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In the present work, a D-galactose-specific lectin with novel N-terminal sequence was purified from  Musca domestica  L. (Diptera: Muscidae) pupae. The purification was performed using affinity chromatography, ultra-filtration, and HPLC. The haemagglutinating activity of  M. domestica  lectin was specifically inhibited by D-galactose. The haemagglutinating activity of this lectin was stable at temperatures up to 65° C and in pH ranging from 4 to 8. Salts including FeCl 3  and MnCl 2  inhibited the haemagglutinating process, whereas NaCl, KCl, CaCl 2 , MgCl 2 , ZnCl 2 , and AlCl 3  did not. By SDS-PAGE, purified  M. domestica  pupae lectin yielded a single band with a molecular weight of 40 kDa, with or without reduction of β-mercaptoethanol, and it could be stained with Alcian Blue 8 GX. The morphology of purified lectin was observed by atomic force microscopy, which indicated that  M. domestica  lectin was an 8.27 nm high, globular shaped glycoprotein with a 1.41 nm high polysaccharide chain. In addition, antiproliferative activity of this lectin against tumor cells K562 and MCF-7 was determined with a colorimetric assay using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide, which showed that the antiproliferative process was time- and dose-dependent with an IC 50  of 5.7 and 6.7 at 24 h, 5.5 and 6.4 at 36 h, 5.2 and 6.5 µM at 48 h, respectively.

journal of insect science

Purification and Characterization of a New D-Galactose-Specific Lectin from the Housefly,<i>Musca domestica</i>, and Its Antiproliferative Effect on Human K562 and MCF-7 Tumor Cells

Purification and Characterization of a New D-Galactose-Specific Lectin from the Housefly,Musca domestica, and Its Antiproliferative Effect on Human K562 and MCF-7 Tumor Cells