ArticlePloS one2013
Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 58 citations in OpenAlex.
- Modification of Soybean 11S Protein by Fermentation: Antioxidant Capacity, Oxidative Stability in Emulsions and Structural Evolution.Foods (Basel, Switzerland) · 2026Article
- Refolding of the Alkali Denatured Bovine Beta-Lactoglobulin by the Synthetic ZnO Nanochaperone: A Useful Technique for Protein Renaturation.ACS omega · 2025Article
- Carbohydrate-Binding Mechanism of the Coagulant Lectin fromMolecules (Basel, Switzerland) · 2024Article
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms.Biomolecules · 2021Article
- Biochemical characterization of a native group III trypsin ZT from Atlantic cod (Gadus morhua).International journal of biological macromolecules · 2019Article
- Identification of Banana Lectin Isoforms and Differential Acetylation Through Mass Spectrometry Approaches.The protein journal · 2018Article
- Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Frontiers in chemistry · 2018Article
- Article
- Banana lectin: a brief review.Molecules (Basel, Switzerland) · 2014Review
- Selective isolation of trypsin inhibitor and lectin from soybean whey by chitosan/tripolyphosphate/genipin co-crosslinked beads.International journal of molecular sciences · 2014Article
- Thermal, chemical and pH induced unfolding of turmeric root lectin: modes of denaturation.PloS one · 2014Article
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8 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Banana lectin (BL) is a homodimeric protein categorized among jacalin-related family of lectins. The effect of acidic pH was examined on conformational stability of BL by using circular dichroism, intrinsic fluorescence, 1-anilino-8-napthalene sulfonate (ANS) binding, size exclusion chromatography (SEC) and dynamic light scattering (DLS). During acid denaturation of BL, the monomerization of native dimeric protein was found at pH 2.0. The elution profile from SEC showed two different peaks (59.65 ml & 87.98 ml) at pH 2.0 while single peak (61.45 ml) at pH 7.4. The hydrodynamic radii (R h) of native BL was 2.9 nm while at pH 2.0 two species were found with R h of 1.7 and 3.7 nm. Furthermore at, pH 2.0 the secondary structures of BL remained unaltered while tertiary structure was significantly disrupted with the exposure of hydrophobic clusters confirming the existence of molten globule like state. The unfolding of BL with different subunit status was further evaluated by urea and temperature mediated denaturation to check their stability. As inferred from high Cm and ΔG values, the monomeric form of BL offers more resistance towards chemical denaturation than the native dimeric form. Besides, dimeric BL exhibited a Tm of 77°C while no loss in secondary structures was observed in monomers even up to 95°C. To the best of our knowledge, this is the first report on monomeric subunit of lectins showing more stability against denaturants than its native dimeric state.
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