ArticleThe protein journal2012
Purification and biological activities of Abelmoschus esculentus seed lectin.
Article in The protein journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 32 citations in OpenAlex.
- Targeting Yeast Pathogens with Lectins: A Narrative Review from Mechanistic Insights to the Need for Addressing Translational Challenges.Biomedicines · 2026Review
- An Overview of the Current Scientific Evidence on the Biological Properties ofFoods (Basel, Switzerland) · 2025Review
- Evaluation of Anti-cancer Potential ofProtein and peptide letters · 2025Article
- The use of African medicinal plants in cancer management.Frontiers in pharmacology · 2023Review
- Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
- Okra (Molecules (Basel, Switzerland) · 2021Review
- The secret of health in daily cuisine: typical healthy vegetables in local markets in central Myanmar.Journal of ethnobiology and ethnomedicine · 2020Article
- Effect of algae and plant lectins on planktonic growth and biofilm formation in clinically relevant bacteria and yeasts.BioMed research international · 2014Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Abelmoschus esculentus (Malvaceae) plant originated in Africa and has spread across a number of tropic countries, including northeastern Brazil. The plant has been used to treat various disorders, such as cancer, microbial infections, hypoglycemia, constipation, urine retention and inflammation. The lectin of A. esculentus (AEL) was isolated by precipitation with ammonium sulfate at a saturation level of 30/60 and purified by ion exchange chromatography (Sephacel-DEAE). The electrophoresis (SDS-PAGE) profile of the AEL showed two protein bands of apparent molecular mass of approximately 15.0 and 21.0 kDa. The homogenity of the protein was confirmed by electrospray mass spectrometry (ESI-MS), which revealed the presence of a 10.29-kDa monomer and a 20.58-kDa dimer. The AEL exhibits agglutinating activity against rabbit (74.41 UH/mP) and human type ABO erythrocytes (21.00 UH/mP). This activity does not require the presence of divalent cations and is specifically inhibited by lactose, fructose and mannose. The intravenous treatment with 0.01, 0.1 and 1 mg/kg of AEL inhibited the paw edema elicited by carrageenan by approximately 15, 22 and 44 %, respectively, but not that induced by dextran. In addition, treatment with 0.1, 1 and 10 mg/kg of AEL also inhibited the abdominal writhing induced by acetic acid by approximately 52, 57 and 69 %, respectively. In conclusion, AEL is a new lectin with a molecular mass of 20.0 kDa, which is -composed of a 10.291-Da monomer and a 20.582-kDa dimer, that exhibits anti-inflammatory, antinociceptive and hemagglutinating activities. In addition, the lectin hemagglutinating property is both metallo-independent and associated with the lectin domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.