Purification and Characterization of a Rhamnose-Binding Chinook Salmon Roe Lectin with Antiproliferative Activity toward Tumor Cells and Nitric Oxide-Inducing Activity toward Murine Macrophages
- Resource Type
- Authors
- Clara Shui Fern Bah; Evandro Fei Fang; Tzi Bun Ng; Sonya Mros; Michelle McConnell; Alaa El-Din A. Bekhit
- Source
- Journal of Agricultural and Food Chemistry. 59:5720-5728
- Subject
- Carcinoma, Hepatocellular
Hemagglutination
Rhamnose
Antineoplastic Agents
Breast Neoplasms
Nitric Oxide
Nitric oxide
Mice
chemistry.chemical_compound
Salmon
Cell Line, Tumor
Lectins
Animals
Humans
Cell Proliferation
Ovum
biology
Molecular mass
Lectin
Rhamnose binding
General Chemistry
Hep G2
Biochemistry
chemistry
Cell culture
Macrophages, Peritoneal
biology.protein
Female
General Agricultural and Biological Sciences
- Language
- ISSN
- 1520-5118
0021-8561
In this study, a rhamnose-binding lectin from the roe of chinook salmon (Oncorhynchus tshawytscha) was purified and characterized, and its biological activities were examined in several model systems. Chinook salmon roe lectin had a molecular mass of 30 kDa and agglutinated rabbit and bovine erythrocytes. The hemagglutination activity of the lectin was not affected by metal ions. The lectin was stable up to 70 °C and between pH 4 and pH 11. Chinook salmon roe lectin did not exert antifungal activity toward the fungal species tested and did not exhibit mitogenic response toward mouse splenocytes up to a concentration of 5 mg/mL. The lectin had selective antiproliferative activity toward human breast cancer MCF-7 cells and hepatoma Hep G2 cells. It also induced the production of nitric oxide from mouse peritoneal macrophages. This is the first report that demonstrates these biological activities from chinook salmon roe lectin.