ArticleGlycoconjugate journal2018
Purification, characterization and fine sugar specificity of a N-Acetylgalactosamine specific lectin from Adenia hondala.
Article in Glycoconjugate journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Review of the ethnobotany, phytochemistry, pharmacology, and toxicity studies of the genusFrontiers in pharmacology · 2025Review
- Lectin-glycan interactions: a comprehensive cataloguing of cancer-associated glycans for biorecognition and bio-alteration: a review.Glycoconjugate journal · 2024Review
- Hemagglutinin from the Root Tuber ofTurkish journal of pharmaceutical sciences · 2024Article
- Article
- In Vitro Phytotherapeutic Properties of Aqueous ExtractedMolecules (Basel, Switzerland) · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Plant lectins are gaining interest because of their interesting biological properties. Several Adenia species, that are being used in traditional medicine to treat many health ailments have shown presence of lectins or carbohydrate binding proteins. Here, we report the purification, characterization and biological significance of N-Acetyl galactosamine specific lectin from Adenia hondala (AHL) from Passifloraceae family. AHL was purified in a single step by affinity chromatography on asialofetuin Sepharose 4B column, characterized and its fine sugar specificity determined by glycan array analysis. AHL is human blood group non specific and also agglutinates rabbit erythrocytes. AHL is a glycoprotein with 12.5% of the carbohydrate, SDS-PAGE, MALDI-TOF-MS and ESI-MS analysis showed that AHL is a monomer of 31.6 kDa. AHL is devoid of DNase activity unlike other Ribosome inactivating proteins (RIPs). Glycan array analysis of AHL revealed its highest affinity for terminal lactosamine or polylactosamine of N- glycans, known to be over expressed in hepatocellular carcinoma and colon cancer. AHL showed strong binding to human hepatocellular carcinoma HepG2 cells with MFI of 59.1 expressing these glycans which was effectively blocked by 93.1% by asialofetuin. AHL showed dose and time dependent growth inhibitory effects on HepG2 cells with IC
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