calystegia sepium/carbohydrate

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Calystegines in Calystegia sepium do not inhibit fungal growth and invertase activity but interact with plant invertase.

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Calystegines are alkaloidal glycosidase inhibitors. They accumulate predominantly in young and meristemic parts of Calystegia sepium (Convolvulaceae). C. sepium, bindweed, infests meadows and cereal fields and is difficult to control chemically. Fungal pathogens against C. sepium are established as

[Enzymes of carbohydrate metabolism in nectaries].

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1. The activity of some important enzymes of carbohydrate metabolism was investigated in several fractions of homogenized tissues of nectaries from Deutzia scabra and Convolvulus sepium in the secretion-phase. Considerable activity was found for the particle-associated hexokinase and the soluble

The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold.

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The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant

Carbohydrate binding properties of banana (Musa acuminata) lectin II. Binding of laminaribiose oligosaccharides and beta-glucans containing beta1,6-glucosyl end groups.

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This paper extends our knowledge of the rather bizarre carbohydrate binding poperties of the banana lectin (Musa acuminata). Although a glucose/mannose binding protein which recognizes alpha-linked gluco-and manno-pyranosyl groups of polysaccharide chain ends, the banana lectin was shown to bind to

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