Isolation and characterization of a lectin from peanut roots

Kalsi, Gurpreet; Das, Hasi R.; Babu, C. R.; Das, Rakha H.

doi:10.1016/0304-4165(92)90067-5

Cited by 28 publications

(8 citation statements)

References 21 publications

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“…Peanut plant has been illustrated for differential distribution of lectins by a number of reports dealing with the isolation and characterization of lectins with different sugar specificities namely seed lectin (PNA, SGL), nodule lectins (NGLa, NGLb), root lectins (PRA I, PRA II and PRA III) and stem lectins (SL-I and SL-II) (Singh and Das 1994;Lotan et al 1975;Kishinevsky et al 1988;Kalsi et al 1992Kalsi et al , 1993Shanker and Das 2001). We focused on peanut lectin SL-I as it is ubiquitously but differentially expressed throughout the plant tissues and hence may throw some light on the preserved inherent biological function of the lectins.…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachis hypogaea) lectin SL-I

et al. 2006

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Isolation and purification of a alpha-methyl-mannoside specific lectin (SL-I) of peanut was reported earlier [Singh and Das (1994) Glycoconj J 11:282-285]. Native SL-I is a glycoprotein having approximately 31 kDa subunit molecular mass and forms dimer. The gene encoding this lectin is identified from a 6-day old peanut root cDNA library by anti-SL-I antibody and N-terminal amino acid sequence homology to the native lectin. Nucleotide sequence derived amino acid sequence of the re-SL-I shows amino acid sequence homology with the N-terminal and tryptic digests' amino acid sequence of the native SL-I (nSL-I). Presence of a putative glycosylation (QNPS) site and a hydrophobic adenine-binding (VLVSYDANS) site is also identified in SL-I. Homology modeling of the lectin suggests it to be an archetype of legume lectins. It is expressed as a approximately 30 kDa apoprotein in E. coli and has the carbohydrate specificity and secondary structure identical to its natural counterpart. The lectin SL-I inhibits cytokinin 6-benzylaminopurine (BA)-induced "delayed leaf senescence" and "cotyledon expansion". Equilibrium dialysis revealed a single high-affinity binding site for adenine (7.6 x 10(-6 )M) and BA (1.09 x 10(-5 )M) in the SL-I dimer and thus suggesting that the cytokinin antagonist effect of SL-I is mediated by the direct interaction of SL-I with BA.

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Section: Discussionmentioning

confidence: 99%

Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachis hypogaea) lectin SL-I

et al. 2006

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“…Apart from PNL, GL, and ML, a fourth lectin is produced by groundnut roots, the glucose‐specific PRAII [134, 135]. The inhibition pattern of its haemagglutinating activity with rabbit erythrocytes is markedly different from that of ML in showing a preference for β ‐linked sugars [136], whereas ML was shown to prefer α ‐linked sugars [127].…”

Section: Molecular Communication Between the Symbiontsmentioning

confidence: 99%

Nodulation of groundnut byBradyrhizobium: a simple infection process by crack entry

1997

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Infection of legumes by rhizobia may occur by immediate intercellular penetration of root cells (crack entry) as an alternative mode to the more elaborate infection through infection threads. The intercellular spreading mode of infection is exemplified through a comprehensive description of root infection by Bradyrhizobium and nodule organogenesis in Arachis hypogaea (groundnut). The role of axillary root hairs and the processes of plant penetration and intercellular spreading, of internalization and intracellular multiplication, and of bacteroid differentiation are described. Then flavonoids and phytoalexins, Nod factors, lectins, and surface poly(oligo)saccharides pass in review. The roles of these various (macro)molecules in the chemical communication between the two symbionts are discussed. Attention is given to special features of groundnut nodules; the presence and functions of oleosomes and other bodies, the presence and functions of nodule lectins, and the evidence for the export of amides from the nodules are discussed. Finally, a speculative model for the groundnut infection process is presented.

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“…5) A few legume lectins have been purified from leaves 7) and roots, 8,9) but most have been identified and purified from the seeds.…”

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confidence: 99%

Purification and cDNA cloning of a lectin and a lectin-like protein from Apios americana Medikus tubers

Kouzuma

Irie

Yamazaki

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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An Apios americana lectin (AAL) and a lectin-like protein (AALP) were purified from tubers by chromatography on Butyl-Cellulofine, ovomucoid-Cellulofine, and DEAE-Cellulofine columns. AAL showed strong hemagglutinating activity toward chicken and goose erythrocytes, but AALP showed no such activity toward any of the erythrocytes tested. The hemagglutinating activity of AAL was not inhibited by mono- or disaccharides, but was inhibited by glycoproteins, such as asialofetuin and ovomucoid, suggesting that AAL is an oligosaccharide-specific lectin. The cDNAs of AAL and AALP consist of 1,093 and 1,104 nucleotides and encode proteins of 302 and 274 amino acid residues, respectively. Both amino acid sequences showed high similarity to known legume lectins, and those of their amino acids involved in carbohydrate and metal binding were conserved.

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Isolation and characterization of a lectin from peanut roots

Cited by 28 publications

References 21 publications

Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachis hypogaea) lectin SL-I

Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachis hypogaea) lectin SL-I

Nodulation of groundnut byBradyrhizobium: a simple infection process by crack entry

Purification and cDNA cloning of a lectin and a lectin-like protein from Apios americana Medikus tubers

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