Quaternary association and reactivation of dimeric concanavalin A

Chatterjee, Anindya; Mandal, Dipak K.

doi:10.1016/j.ijbiomac.2005.01.005

Cited by 13 publications

(5 citation statements)

References 38 publications

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“…Concanavalin A was dissociated and reassociated as reported previously. 30 Dissociation into dimer units was accomplished using 8 M urea in a sodium acetate buffer (2 μM protein in 20 mM buffer, pH 5.2, with 0.15 M NaCl, 1 mM Mn 2+ , and 1 mM Ca 2+ ). This mixture was stirred at 25 °C with a constant pH of 4.8 for 18 h. The solution was then centrifuged and the resulting pellet washed with phosphate buffer saline solution (10 mM with a pH of 7.4) and lyophilized.…”

Section: Methodsmentioning

confidence: 99%

“…Concanavalin A was dissociated and reassociated as reported previously . Dissociation into dimer units was accomplished using 8 M urea in a sodium acetate buffer (2 μM protein in 20 mM buffer, pH 5.2, with 0.15 M NaCl, 1 mM Mn 2+ , and 1 mM Ca 2+ ).…”

Section: Methodsmentioning

confidence: 99%

“…The activity of reassociated Con A was tested, as has been previously reported. , A Sephadex G-100 column with a 2 mL bed volume was equilibrated overnight with 20 mM sodium acetate buffer (pH 5.2 with 0.15 M NaCl, 1 mM Mn 2+ , and 1 mM Ca 2+ ) and then loaded with a 1 mL aliquot of released protein (before and after the particles were exposed to pepsin). Unbound protein was collected within 2 min, and the bound protein was eluted using a 0.2 M glucose solution in the 20 mM sodium acetate buffer.…”

Section: Methodsmentioning

confidence: 99%

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Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles

et al. 2017

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Mesoporous silica nanoparticles (MSN) with enlarged pores were prepared and characterized, and reversibly dissociated subunits of concanavalin A were entrapped in the mesopores, as shown by multiple biochemical and material characterizations. When loaded in the MSN, we demonstrated protein stability from proteases and, upon release, the subunits reassociated into active proteins shown through mannose binding and o-phthalaldehyde fluorescence. We have demonstrated a versatile and facile method to load homomeric proteins into MSN with potential applications in enhancing the delivery of large therapeutic proteins.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles

et al. 2017

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“…It exists in the tetrameric form at pH 7.4 and at pH below 6.0 found in the diameter form. 34 The tetramer is joined by two identical homodimer and each monomer is having one saccharides and two metal (Ca 2+ and Mn 2+ ) binding sites. 35,36 Each monomer comprised of 12 b-sheet secondary structure and jelly roll motif like tertiary structure.…”

Section: Introductionmentioning

confidence: 99%

Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH

Khan

Ali

et al. 2016

RSC Adv.

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“…It has also been reported that the anti-insect activity as well as binding and phagocytosis of microorganisms in animals has generally been observed in the case of GlcNAc and mannose specific lectins [6] , [7] , [8] , [9] . Consequently, to aid in the understanding of their function and in designing mimics, there is also an increasing interest in the molecular structure of plant lectins in relation to their functions [10] .…”

Section: Introductionmentioning

confidence: 99%

Thermal, Chemical and pH Induced Unfolding of Turmeric Root Lectin: Modes of Denaturation

Biswas

Chattopadhyaya

2014

PLoS ONE

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Curcuma longa rhizome lectin, of non-seed origin having antifungal, antibacterial and α-glucosidase inhibitory activities, forms a homodimer with high thermal stability as well as acid tolerance. Size exclusion chromatography and dynamic light scattering show it to be a dimer at pH 7, but it converts to a monomer near pH 2. Circular dichroism spectra and fluorescence emission maxima are virtually indistinguishable from pH 7 to 2, indicating secondary and tertiary structures remain the same in dimer and monomer within experimental error. The tryptophan environment as probed by acrylamide quenching data yielded very similar data at pH 2 and pH 7, implying very similar folding for monomer and dimer. Differential scanning calorimetry shows a transition at 350.3 K for dimer and at 327.0 K for monomer. Thermal unfolding and chemical unfolding induced by guanidinium chloride for dimer are both reversible and can be described by two-state models. The temperatures and the denaturant concentrations at which one-half of the protein molecules are unfolded, are protein concentration-dependent for dimer but protein concentration-independent for monomer. The free energy of unfolding at 298 K was found to be 5.23 Kcal mol−1 and 14.90 Kcal mol−1 for the monomer and dimer respectively. The value of change in excess heat capacity upon protein denaturation (ΔCp) is 3.42 Kcal mol−1 K−1 for dimer. The small ΔCp for unfolding of CLA reflects a buried hydrophobic core in the folded dimeric protein. These unfolding experiments, temperature dependent circular dichroism and dynamic light scattering for the dimer at pH 7 indicate its higher stability than for the monomer at pH 2. This difference in stability of dimeric and monomeric forms highlights the contribution of inter-subunit interactions in the former.

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Quaternary association and reactivation of dimeric concanavalin A

Cited by 13 publications

References 38 publications

Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles

Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles

Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH

Thermal, Chemical and pH Induced Unfolding of Turmeric Root Lectin: Modes of Denaturation

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