Purification and Characterization of Two Lectins from Callus of<i>Helianthus tuberosus</i>

Nakagawa, Ryoji; Yasokawa, Daisuke; Ikeda, Takayuki; Nagashima, Koji

doi:10.1271/bbb.60.259

Cited by 29 publications

(24 citation statements)

References 2 publications

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“…In a similar manner, other groups (Nakagawa et al 1996;Zhang et al 2000) have successfully applied acidic extraction methods for the puriWcation of lectins. As discussed in Peumans et al (2000b), this is a key feature in the puriWcation of certain lectins from other plant species due to the reversible loss of sugar-binding at an acidic pH.…”

Section: Discussionmentioning

confidence: 95%

Purification and characterisation of a jacalin-related, coleoptile specific lectin from Hordeum vulgare

Grunwald

Heinig

Thole

et al. 2007

Planta

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A plant lectin was isolated from barley (Hordeum vulgare) coleoptiles using acidic extraction and different chromatographic methods. Sequencing of more than 50% of the protein sequence by Edman degradation confirmed a full-length cDNA clone. The subsequently identified open reading frame encodes for a 15 kDa protein which could be found in the soluble fraction of barley coleoptiles. This protein exhibited specificity towards mannose sugar and is therefore, accordingly named as Horcolin (Hordeum vulgare coleoptile lectin). Database searches performed with the Horcolin protein sequence revealed a sequence and structure homology to the lectin family of jacalin-related lectins. Together with its affinity towards mannose, Horcolin is now identified as a new member of the mannose specific subgroup of jacalin-related lectins in monocot species. Horcolin shares a high amino acid homology to the highly light-inducible protein HL#2 and, in addition to two methyl jasmonic acid-inducible proteins of 32.6 and 32.7 kDa where the jasmonic acid-inducible proteins are examples of bitopic chimerolectins containing a dirigent and jacalin-related domain. Immunoblot analysis with a cross-reactive anti-HL#2 antibody in combination with Northern blot analysis of the Horcolin cDNA revealed tissue specific expression of Horcolin in the coleoptiles. The function of Horcolin is discussed in the context of its particular expression in coleoptiles and is then compared to other lectins, which apparently share a related response to biotic or abiotic stress factors.

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Section: Discussionmentioning

confidence: 95%

Purification and characterisation of a jacalin-related, coleoptile specific lectin from Hordeum vulgare

Grunwald

Heinig

Thole

et al. 2007

Planta

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“…The hemagglutination titre of the protein sample incubated in PBS, pH 7.2, served as the control. Percentage of hemagglutinating activity was calculated according to Nakagawa et al (1996).…”

Section: Assay Of Hemagglutinating Activitymentioning

confidence: 99%

Anti-insect potential of a lectin from the tuber, Dioscorea mangenotiana towards Eldana saccharina (Lepidoptera: Pyralidae)

Akinyoola¹,

Odekanyin²,

Kuku³

et al. 2016

J. Agric. Biotech. Sustain. Dev.

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A lectin was purified from the tuber, Dioscorea mangenotiana in this study. The lectin agglutinated erythrocytes from human and rabbit, and the activity was inhibited by glucose and N-acetyl-Dglucosamine with minimum inhibitory concentration (MIC) of 50 and 25 mM, respectively. The lectin was composed of two isoforms, DML I and DML II. The apparent native molecular mass of DML I was estimated at 51 kDa and the subunit molecular mass at 25 kDa, suggesting a dimeric structure. The lectin was stable up to 90°C and within the physiological pH range. The lectin when incorporated in artificial diet at concentrations of 10 to 160 µg ml -1 and fed ad libitum to the second instar larvae of Eldana saccharina, prolonged the development period and significantly inhibited the pupation and emergence of the insect in a dose-dependent manner. The LC 50 calculated based on mortality after 72 h of treatment was 66.6 mg/ml. The activities of hydrolytic enzymes -acid phosphatase, alkaline phosphatase and acetylcholine esterase in the larvae reared on diet containing lethal dose of the lectin were significantly affected as compared to those fed on diet without the lectin. The results showed that DML I has promising anti-insect potential and could be employed in a biotechnological strategy for the pest management.

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“…For the heat stability test, the TBL solutions were heated at different temperatures (25°C-80°C) for 30 min and immediately cooled on ice. Cooled solutions were then assayed for hemagglutinating activity (Nakagawa et al, 1996).…”

Section: Temperature and Ph Stability On Hemagglutinating Activity Ofmentioning

confidence: 99%

Stimulation of dendritic cell maturation and induction of apoptosis in lymphoma cells by a stable lectin from buckwheat seeds

Bai¹,

Ji²,

Feng³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. The present study aims to purify and characterize lectin from tartary buckwheat seeds and study its properties as well as biological activities to determine its possible biomedical applications in promoting maturation and proliferation of peripheral blood DCs derived from healthy donors and to study the effect of inducing apoptosis in human leukemia U937 cells. A novel tartary buckwheat lectin (TBL) protein, purified from tartary buckwheat seeds, showed a single band with a molecular mass of 65 kDa in SDS-PAGE. The purified TBL hemagglutinated both human and animal erythrocytes and showed preference for blood type O and the rabbit blood type. TBL is active at up to 60°C, and it is acid-and alkali-stable. TBL (25 μg/mL) combined with 5 x 10 -5 M rhIL-4 promotes maturation and proliferation of peripheral blood dendritic cells (DCs), which is stronger than that promoted by rhTNF-α (20 ng/mL). Exposure of DCs to 50 μg/ mL TBL for 48 h resulted in extensive upregulation of maturation (2015) markers CD83 and CD40. These TBL-DCs were capable of producing several pro-inflammatory cytokines such as interleukin-10 (IL-10) and interleukin-12 (IL-12). The results of the treatment of human leukemia U937 cells with TBL in doses of 12.5, 25, 50, and 100 μg/mL showed that tartary buckwheat-derived lectin induces apoptosis in a dosedependent manner. Our results encourage the use of tartary buckwheat and tartary buckwheat-derived lectins as immunopotentiating foods, targeted to strengthen immune responses and display a potential dietary supplement for cancer prevention.

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Purification and Characterization of Two Lectins from Callus ofHelianthus tuberosus

Cited by 29 publications

References 2 publications

Purification and characterisation of a jacalin-related, coleoptile specific lectin from Hordeum vulgare

Purification and characterisation of a jacalin-related, coleoptile specific lectin from Hordeum vulgare

Anti-insect potential of a lectin from the tuber, Dioscorea mangenotiana towards Eldana saccharina (Lepidoptera: Pyralidae)

Stimulation of dendritic cell maturation and induction of apoptosis in lymphoma cells by a stable lectin from buckwheat seeds

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