Lectin synthesis in developing and germinating wheat and rye embryos

Peumans, Willy J.; Stinissen, Hetty M.; Carlier, Albert R.

doi:10.1007/bf00393441

Cited by 35 publications

(14 citation statements)

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“…2, the precipitin lines formed with WGA and AREL fuse completely, indicating that both embryo lectins are antigenically very closely related. Previous work on cereal embryo lectins revealed that wheat, rye and barley lectins are structurally so closely related that they can exchange subunits with each other in vitro and in vivo [19]. Since WGA and AREL were apparently very similar, both structurally and serologically, experiments were set up to find out wether these two lectins too were able to exchange subunits in vitro.…”

Section: Agropyrum Repcns Embryo Lectin (Arel)mentioning

confidence: 99%

“…Since WGA and AREL were apparently very similar, both structurally and serologically, experiments were set up to find out wether these two lectins too were able to exchange subunits in vitro. Actually, CLAA (which corresponds to the WGA isolectin composed of two identical subunits coded for by the A genome of hexaploid wheat) was used in stead of complete WGA since the latter is already a mixture of six different isolectins [18]. As shown in Fig.…”

Section: Agropyrum Repcns Embryo Lectin (Arel)mentioning

confidence: 99%

“…Additional experiments with rabbit erythrocytes and human lymphocytes indicated that with these cell types too, ARLL is inhibited exclusively by GlcNAc and ( G~c N A c )~ (Table 5). Therefore, it is likely that the preferential agglutination of group A erythrocytes results from binding of ARLL to terminal GalNAc residues on the [19]. In control experiments, lectins were dialyzed separately and combined just before loading on the ion-exchange column.…”

Section: Comparison Of Agglutination Properties Ofpurified a R L L mentioning

confidence: 99%

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A new type of cereal lectin from leaves of couch grass (Agropyrum repens)

Cammue

Stinissen

Peumans

1985

European Journal of Biochemistry

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Extracts from couch grass (Agropyrum repens) leaves contain relatively high lectin concentrations. Preliminary experiments with crude extracts indicated that the leaf lectin differs from the embryo lectin of the same species and other Gramineae embryo lectins with respect to its sugar and blood group specificity, and serological properties. A comparison of the biochemical, physicochemical and biological properties of purified lectins from couch grass leaves and embryos, and wheat germ agglutinin revealed that the leaf lectin has the same molecular structure as the embryo lectins. It is a dimer composed of two identical subunits, which, however, are slightly larger than embryo lectin subunits. Structural differences between both couch grass lectins were further inferred from in vitro subunit exchange experiments and serological analyses. Whereas the embryo lectin readily forms heterodimers with embryo lectins from other cereal species and also is serologically indistinguishable from them, the leaf lectin does not exchange subunits with the same embryo lectins and is serologically different. In addition, couch grass leaf lectin exhibits specificity for N-acetylgalactosamine and agglutinates preferentially blood-group-A erythrocytes whereas the embryo lectin is not inhibited by N-acetylgalactosamine and exhibits no blood-group specificity. It was observed also that the lectin content of couch grass leaves varies enormously during the seasons.

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Section: Agropyrum Repcns Embryo Lectin (Arel)mentioning

confidence: 99%

Section: Agropyrum Repcns Embryo Lectin (Arel)mentioning

confidence: 99%

Section: Comparison Of Agglutination Properties Ofpurified a R L L mentioning

confidence: 99%

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A new type of cereal lectin from leaves of couch grass (Agropyrum repens)

Cammue

Stinissen

Peumans

1985

European Journal of Biochemistry

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“…Then the homogenates were centrifuged (3,000g; 2 min) and the supernatant taken off. Three aliquots of 25 gl were withdrawn for determination of total protein synthesis (measured as incorporation of [35S]cysteine into hot TCA-insoluble material) as described previously (11). To the remainder, an equal volume of Na-acetate buffer (50 nm Na-acetate, 0.1 M NaCl) was added and kept in ice for 30 min.…”

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confidence: 99%

“…To the remainder, an equal volume of Na-acetate buffer (50 nm Na-acetate, 0.1 M NaCl) was added and kept in ice for 30 min. Then the coagulated material was spun off(5 min, 3,000g) and the resulting supernatant used for affinity chromatography of the lectin on immobilized N-acetylglucosamine (Selectin 1 from Pierce Chemical Company, Rockford, IL) as described previously (11 Blue in a mixture of acetic acid:methanol:water (1:5:5, by vol). Thereafter, the gels were destained with the same solvent.…”

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Lectin in Vegetative Tissues of Adult Barley Plants Grown under Field Conditions

Cammue¹,

Stinissen²,

Peumans³

1985

Plant Physiol.

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A study of the distribution of lectins over different vegetative tissues of barley (Hordeum vulgare L.) plnts, which were grown under normal crop conditions, indicated that lectin occurs in roots, leaves, and developing ears. Isolation and characterization of both root and leaf lectins led to the conclusions (a) that they are indistinguishable from the embryo lectin and (b) that the total lectin content of these vegetative organs is many times higher than that of the embryo. Finally, in vivo labeling experiments demonstrated that the lectin is synthesized de novo in roots and leaves.Cereal lectins are a group of closely related proteins occurring in embryos of species belonging to the Triticeae tribe of the Gramineae family (14). At present, three such lectins have been isolated from wheat germ (1) and rye and barley embryos (10), respectively. They not only have the same molecular structure and carbohydrate-binding specificity but are serologically also indistinguishable from each other.Although cereal seed lectins are considered as embryo-specific proteins which are almost exclusively synthesized in the primary axes during seed formation (11), it is becoming increasingly apparent that, at least, WGA2 occurs also in developing seedlings and adult plants. Mishkind et al. (6) found that within a period of 34 d the amount oflectin in wheat plants remains high relative to levels found in ungerminated grains. Further studies indicated that the lectin is located in the roots and shoot base, and in addition is limited to those organs which become exposed to the soil during germination and growth (7,8,13). Moreover, the WGA-like material from adult wheat plants could not be distinguished from authentic WGA with respect to its molecular structure, sugar-binding specificity, and serological properties (8,13 wise). At the end of the labeling period, the incubation medium was taken off and the root tips washed 4 times with 0.1 ml of ice-cold water. Then they were transferred onto a filter and washed with at least 25 ml of ice-cold water. Five leaves were cut from intact plants under water (to avoid penetration of air in the vascular bundles) and transferred into a test tube containing 0.5 ml nutrient medium supplemented with 1.8 MBq [35S]cysteine and incubated for 6 h at 25°C under illumination. At the end of the incubation, leaves were taken off and extensively washed with ice-cold water. Root tips and leaves were homogenized in a cold mortar in 1.5 and 5 ml, respectively, of PBS. Then the homogenates were centrifuged (3,000g; 2 min) and the supernatant taken off. Three aliquots of 25 gl were withdrawn for determination of total protein synthesis (measured as incorporation of [35S]cysteine into hot TCA-insoluble material) as described previously (11). To the remainder, an equal volume of Na-acetate buffer (50 nm Na-acetate, 0.1 M NaCl) was added and kept in ice for 30 min. Then the coagulated material was spun 384 www.plantphysiol.org on May 10, 2018 -Published by Downloaded from

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Seed Germination

Raghavan¹

2000

Developmental Biology of Flowering Plants

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Lectin synthesis in developing and germinating wheat and rye embryos

Cited by 35 publications

References 10 publications

A new type of cereal lectin from leaves of couch grass (Agropyrum repens)

A new type of cereal lectin from leaves of couch grass (Agropyrum repens)

Lectin in Vegetative Tissues of Adult Barley Plants Grown under Field Conditions

Seed Germination

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