Purification and characterization of two major lectins fromVigna mungo (blackgram)

Suseelan, K. N.; Bhatia, Amit; Mitra, R.

doi:10.1007/bf02703190

Cited by 23 publications

(15 citation statements)

References 31 publications

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“…Whereas lectins from Vigna mungo (Suseelan et al 1997) and Erythrinaveluntina, Jackfruit (Artocarpus integrifolia) lectins (Ahmed & Cahtterjee 1987) were stable at 70°C. Lectins from CP leaves and fruits are stable upto 50°C and 60°C respectively.…”

Section: Discussionmentioning

confidence: 99%

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Isolation and characterization of hemagglutinins from Clerodendrum phlomidis L.f.

Khagar¹,

Khagar²,

Pingle³

et al. 2017

Trop. Plant Res.

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Abstract:Lectins from the leaves, fruit, calyx and stem of Clerodendrum phlomidis plant were isolated after screening of total 54 plants from central India. The crude extract of leaves, fruit, calyx and stem of C. phlomidis plant was purified by ammonium sulfate precipitation, followed by dialysis. The isolated lectins of C. phlomidis plant were able to agglutinate human as well as dog, hen, goat mouse, mice and fish erythrocytes. The isolated lectins were found to be lactose specific. The pH stability of C. phlomidis leaves lectins was between 4-10 pH, for fruit lectins it was 5-7 pH, and for calyx and stem lectins it was found stable in between 4 and 8 pH. The calyx and stem lectins were active until 60ºC, fruit has shown activity upto 50ºC and in case of leaves, it was found maximum 40ºC. Beyond their respective optimum temperature and pH range, all the lectins were unable to agglutinate erythrocytes. Hemagglutination activity of C. phlomidis plant lectins was also checked in the presence of different metal ions and it was found that it was partially inhibited by aluminium metal ion.

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Section: Discussionmentioning

confidence: 99%

“…During assay 100 μl of the extract was incubated with pH buffers for 30 minutes at room temperature and hemagglutination activity was determined against 2% RBC's. Optimization of pH was determined by plotting graph of pH range against percent agglutination (Suseelan et al 1997).…”

Section: Characterization Of Cp Lectins Optimization Of Ph For Hemaggmentioning

confidence: 99%

Isolation and characterization of hemagglutinins from Clerodendrum phlomidis L.f.

Khagar¹,

Khagar²,

Pingle³

et al. 2017

Trop. Plant Res.

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“…2M glycine -HCl buffer, for pH 4 & 5: 0.2M sodium acetate buffer, for pH 6 & 7: 0.2M sodium phosphate buffer, for pH 8: 0.2M Tris HCl buffer, for pH 9: 0.2M glycine-NaOH buffer and for pH 10 & 13: 0.2M carbonate-bicarbonate buffers were used. 100 µl of lectin was incubated with 100 µl of different buffer solutions for 30 minutes at room temperature and then assayed for agglutination with 2% erythrocytes (Suseelan et al 1997).…”

Section: Ph Stability Studiesmentioning

confidence: 99%

Isolation and characterization of lectin from the leaves of Euphorbia tithymaloides (L.)

Jawade¹,

Pingle²,

Tumane³

et al. 2016

Trop. Plant Res.

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Lectins or glycoproteins from the leaves of Euphorbia tithymalo were isolated after screening of different flora from Central India. The crude extract of leaves was dialyzed andammonium sulfate precipitation done and followed by dialysis for the purification of lectins. Protein concentration in the purified extract was 10 mg.ml -1 measured by Biuret Method. The purified lectins were able to agglutinate human erythrocytes of ABO blood group system. Agglutination was also visible with animal erythrocytes. Lectin of ET was Galactose/Lactose specific and shows maximum activity at pH-7 and temperature between 40-60º C. Molecular weight of purified extract of ET was determined by 1D-SDS Polyacrylamide gel electrophoresis which was found to be 70.24, 28.53 and 14.68 kDa.

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“…Lectins were also reported in callus tissues and cell cultures [6][7][8][9]. Few lectins have been found to be enzymatic, possessing α-and β-galactosidase activities [10][11][12][13][14]. Most legume lectins are oligomeric [15] and are synthesized on the rough endoplasmic reticulum, where they undergo cotranslational and/or posttranslational modifications before reaching their final destination, the protein bodies [16].…”

Section: Introductionmentioning

confidence: 98%

“…There were three monomeric lectin species having relative molecular weights (M r ) of 94, 89, and 83 kDa showing D-galactose specificity. All the three lectins were enzymatic, with multiple carbohydrate-binding sites [13]. The lectins of M r 94 and 83 had α-galacosidase activity, while M r 89 kDa lectin showed β-galactosidase activity.…”

Section: Introductionmentioning

confidence: 99%

The In Vivo Synthesis and Accumulation of Lectin in Developing Seeds of Black Gram (Vigna mungo L. Hepper)

Suseelan

Mitra²,

Bhatia³

et al. 2004

Plant Foods Hum Nutr

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Black gram (Vigna mungo L. Hepper) seed contains two D-galactose-specific lectin species, BGL-I and BGL-II, identified on the basis of elution from ion exchange column and immunochemical cross-reactivity. BGL-I consisted of two monomeric lectins, BGL-I-1 and BGL-1-2, of relative molecular weights 94 and 89 kDa, respectively. BGL-II is another monomeric lectin with a molecular weight of 83 kDa. The in vivo synthesis studies using pulse-chase experiment showed that BGL-II lectin was synthesized as early as 14 days after flowering (DAF). The 94-kDa BGL-I-1 lectin was synthesized around 17 DAF. There was no cotranslational or posttranslational modification of the lectin proteins. The amount of lectin in developing seeds was determined by radial immunodiffusion assay technique. The maximum amount of lectin per seed was found at 28 DAF.

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Purification and characterization of two major lectins fromVigna mungo (blackgram)

Cited by 23 publications

References 31 publications

Isolation and characterization of hemagglutinins from Clerodendrum phlomidis L.f.

Isolation and characterization of hemagglutinins from Clerodendrum phlomidis L.f.

Isolation and characterization of lectin from the leaves of Euphorbia tithymaloides (L.)

The In Vivo Synthesis and Accumulation of Lectin in Developing Seeds of Black Gram (Vigna mungo L. Hepper)

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