Dextran Raffinose Derivative Assay for Affinity Purified Corn Coleoptile Lectin

Merida, Adriana; Vasquez, Leonardo; Martínez, Marta Gil; Aquino, Teresa; Pérez-Campos, Eduardo; Córdoba, Félix

doi:10.1271/bbb.60.2064

Cited by 3 publications

(1 citation statement)

References 2 publications

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“…The galactose-specific lectin from corn (Z. mays) coleoptile (CCL) was purified by affinity chromatography [15,16]. Concanavalin A (Con A) from Cana6alia ensiformis, specific for mannose/glucose (Man/Glc) was purified by affinity chromatography according to Agrawal and Goldstein [17].…”

Section: Methodsmentioning

confidence: 99%

Effect of plant lectins on Ustilago maydis in vitro

Santiago

Saavedra

Campos

et al. 2000

CMLS, Cell. Mol. Life Sci.

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Ustilago maydis is an edible parasitic basidiomycete, which specifically infects corn (Zea mays) and teocintle (Z. diploperennis). To characterise the interaction between the basidiomycete and its host organism, we tested the effect of plant lectins with well-known sugar specificity on the growth and germination of U. maydis spores. Lectins specific for N-acetyl-D-galactosamine, such as those from Dolichos biflorus and Phaseolus lunatus, and the wheatgerm agglutinin specific for N-acetyl-D-glucosamine inhibited spore germination, but were ineffective in modifying U. maydis cell growth. The galactose-specific lectin from the corn coleoptyle inhibited both germination and cell growth, while the lectin concanavalin A (mannose/glucose specific) activated spore germination and growth. Our results suggest that specific saccharide-containing receptors participate in regulating the growth and maturation of U. maydis spores.

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Section: Methodsmentioning

confidence: 99%

Effect of plant lectins on Ustilago maydis in vitro

Santiago

Saavedra

Campos

et al. 2000

CMLS, Cell. Mol. Life Sci.

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Isolation of Fully Active and Stable Corn Coleoptile Lectins

Martínez

Córdoba²

2000

Preparative Biochemistry and Biotechnology

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It appears that the reason for the lack of information and data about corn coleoptile lectin is due to the instability of preparation with a rapid loss of hemagglutinating activity and abundant precipitate. In this paper, we assayed phosphate, borate, tris, and ascorbate-sucrose extraction buffers to compare lectin activity and protein yield. The ascorbate-sucrose buffer (AS-buffer) proved to be the best extracting solution. In a second step, cold acetone was employed to concentrate crude lectin. An increase of specific activity from the first to the third acetone precipitation was obtained. The protective effect on hemagglutinating activity of AS-buffer led us to test cysteine, metabisulfite, borohydride, and dithiothreitol (DTT) as reducing agents. The compounds were ineffective. Dissociating gel electrophoresis of the acetone-purified lectin disclosed a band pattern of components around 60 kD, a second band at 29 kD, and minor bands close to 15 KD. The procedure is useful for the preparation of stable, high activity corn coleoptile lectin. Further purification using affinity chromatography, as in reference (1) could become a major advance to obtain corn lectin of adequate purity for sequential analysis.

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Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Santizo

Zenteno

Pina-Canseco

et al. 2009

Tohoku J. Exp. Med.

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The human coagulation factor VIII (FVIII) is an essential cofactor for the proteolytic activation of factor X. FVIII is activated by thrombin and blood coagulation factor Xa; factor IXa (FIXa) activates factor X (FXa), requiring Ca 2+ , phospholipids, and activated Factor VIII (FVIIIa) (Schmidt et al. 2005). FVIII and von Willebrand factor (VWF) form a non-covalently bound complex. This complex (FVIII/ VWF) circulates in the human plasma, is critical to homeostasis, and normally exists in inactive form. The binding of FVIII to VWF is essential for the survival of FVIII in vivo (Kaufman and Pipe 1999). Deficiencies or structural defects in FVIII are responsible for the most common inherited bleeding disorders, such as hemophilia and von Willebrand disease (Lillicrap 2008).FVIII is a polypeptide of 2332 amino acids, synthesized in the liver by parenchyma cells and hepatic sinusoidal endothelium cells, as well as by the pulmonary endothelium. FVIII has several glycosylation sites that appear to be important in its circulation kinetics. This factor possesses N-glycosydically linked glycans, which are characterized by a N-acetyl-glucosamine (GlcNAc)-asparagine inner core and are relevant for the folding and productive secretion of FVIII, and O-glycosydically glycans, which are characterized by N-acetyl-galactosamine (GalNAc)-serine/threonine and are involved in determining protein conformation and interact with other glycoproteins. FVIII possesses two unusual mannosylated sites that can be recognized by mannose receptors on Kupffer cells (Dasgupta et al. 2007).

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Dextran Raffinose Derivative Assay for Affinity Purified Corn Coleoptile Lectin

Cited by 3 publications

References 2 publications

Effect of plant lectins on Ustilago maydis in vitro

Effect of plant lectins on Ustilago maydis in vitro

Isolation of Fully Active and Stable Corn Coleoptile Lectins

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

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