Characterization of Con C, a lectin from Canavalia cathartica Thouars seeds

Suseelan, K. N.; Bhagwath, Arun; Pandey, R.; Gopalakrishna, T.

doi:10.1016/j.foodchem.2006.11.064

Cited by 13 publications

(9 citation statements)

References 31 publications

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“…3(A)), suggesting different conformational changes of the lectin under these conditions. This phenomenon, although not the exact temperature shift values, is quite similar to that seen for the lectin from Phaseolus vulgaris ,29 which is extremely thermostable at temperatures around 82 °C, for the lectin from Astragalus mongholicus , which is still active at 65 °C,30 and for the lectin from C. cathartica , which is active at 60 °C but not at 70 °C 25…”

Section: Resultssupporting

confidence: 72%

“…In addition, it showed a weak but essentially non‐specific agglutination of human erythrocytes, where the A, B and AB groups showed an equal agglutination activity and group O was only marginally stronger than the other three human groups, but still weak and on a par with that seen against mouse and guinea pig erythrocytes. The low haemagglutinating activity of this lectin towards mouse and guinea pig erythrocytes is similar to that seen with the lectins from Pisum sativum and Bauhinia monandra seeds,22, 23 while the high haemagglutinating activity seen with rabbit erythrocytes is broadly similar to that observed with the lectins from Hevea brasiliensis and Canavalia cathartica 24, 25. However, the combined species–activity profile of the lectin from K. parviflora is somewhat unique.…”

Section: Resultssupporting

confidence: 66%

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A thermostable lectin from the rhizomes ofKaempferia parviflora

Konkumnerd

Karnchanatat

Sangvanich

2010

J. Sci. Food Agric.

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Section: Resultssupporting

confidence: 72%

Section: Resultssupporting

confidence: 66%

A thermostable lectin from the rhizomes ofKaempferia parviflora

Konkumnerd

Karnchanatat

Sangvanich

2010

J. Sci. Food Agric.

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“…While lectin retained its full hemagglutinating activity up to 80°C for 30 min, PTL retained its full hemagglutinating activity in the broad pH range of pH 5 to 12. In addition, the activities of some other lectins are diminished above pH 9 reportedly (kaur et al [2005]; Suseelan et al [2007]; Vaz et al [2010]).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a novel plant lectin from Pinellia ternata with antineoplastic activity

et al. 2012

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A novel Pinellia ternata lectin was purified from the bulbs of a Chinese herb Pinellia ternata using a combination of hydrophobic chromatography and DEAE-ion exchange chromatography. The lectin was found to be a homodimer of 12093.3 Da subunits as determined by gel filtration and MS. Biochemical characterization of the lectin revealed the existence of a glycoprotein, which contains 3.22% neutral sugars. The N-terminal 10-amino acid sequence of the lectin, QGVNISGQVK, has not been reported for other lectins. The lectin had a special agglutinating activity with mouse erythrocytes at a minimum concentration of 8.0 ug/ml. The lectin was stable in the pH range of pH 5–12 and temperatures up to 80°C for 30 min. The results of MTT experiment showed that the lectin had significant effect towards tumor cells, the maximum inhibition of cell proliferation with Sarcoma 180, HeLa and K562 cell line were 85.2%, 74.6% and 59.4% respectively. Experimental therapy in vivo also showed that PTL apparently inhibited transplanted tumor in mice. Flow cytometric analysis demonstrated that PTL inhibited the proliferation of Sarcoma 180 in a time- and dose-dependent manner through inhibiting the transition of G1/S and subsequently inducing G0/G1 cell cycle arrest. Thus, Pinellia ternata lectin displays a high potential for antitumor activity.

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“…These data suggest that CoxyL, in contrast to various other leguminous lectins Loris et al, 1998), does not need divalent cations for its activity, as they are most probably tightly bound to the protein. Although this property is especially rare in the case of lectins from the Diocleinae subtribe, the hemagglutinating activity of other Diocleinae lectins, such as those from Canavalia cathartica, was also unaffected by EDTA (Suseelan et al, 2007).…”

Section: Effects Of Ph Temperature and Divalent Ions On Lectin-indumentioning

confidence: 99%

Purification, characterization and partial sequence of a pro‐inflammatory lectin from seeds of Canavalia oxyphylla Standl. & L. O. Williams

Santiago

Leitão

Pereira

et al. 2014

J of Molecular Recognition

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Recent studies have shown that lectins are promising tools for use in various biotechnological processes, as well as studies of various pathological mechanisms, isolation, and characterization of glycoconjugates and understanding the mechanisms underlying pathological mechanisms conditions, including the inflammatory response. This study aimed to purify, characterize physicochemically, and predict the biological activity of Canavalia oxyphylla lectin (CoxyL) in vitro and in vivo. CoxyL was purified by a single-step affinity chromatography in Sephadex® G-50 column. Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that the pure lectin consists of a major band of 30 kDa (α-chain) and two minor components (β-chain and γ-chain) of 16 and 13 kDa, respectively. These data were further confirmed by electrospray ionization mass spectrometry, suggesting that CoxyL is a typical ConA-like lectin. In comparison with the average molecular mass of α-chain, the partial amino acid sequence obtained corresponds to approximately 45% of the total CoxyL sequence. CoxyL presented hemagglutinating activity that was specifically inhibited by monosaccharides (D-glucose, D-mannose, and α-methyl-D-mannoside) and glycoproteins (ovalbumin and fetuin). Moreover, CoxyL was shown to be thermostable, exhibiting full hemagglutinating activity up to 60°C, and it was pH-sensitive for 1 h, exhibiting maximal activity at pH 7.0. CoxyL caused toxicity to Artemia nauplii and induced paw edema in rats. This biological activity highlights the importance of lectins as important tools to better understand the mechanisms underlying inflammatory responses.

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Characterization of Con C, a lectin from Canavalia cathartica Thouars seeds

Cited by 13 publications

References 31 publications

A thermostable lectin from the rhizomes ofKaempferia parviflora

A thermostable lectin from the rhizomes ofKaempferia parviflora

Purification and characterization of a novel plant lectin from Pinellia ternata with antineoplastic activity

Purification, characterization and partial sequence of a pro‐inflammatory lectin from seeds of Canavalia oxyphylla Standl. & L. O. Williams

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