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I C Dea

Publications and source records attributed to I C Dea.

6 recordsLinked to original sources
PubMed1988

A beta-D-galactosidase from nasturtium (Tropaeolum majus L.) cotyledons. Purification, properties, and demonstration that xyloglucan is the natural substrate.

beta-D-Galactosidase activity has been detected previously in the cotyledons of germinated nasturtium (Tropaeolum majus L.) seeds and has been linked to the hydrolysis in vivo of storage xyloglucan (amyloid) (Edwards, M., Dea, I. C. M., Bulpin, P. V., and Reid, J. S. G. (1985) Planta (Berl.) 163, 133-140). The major beta-D-galactosidase present in extracts from the cotyledons of 9-day seedlings has now been purified to apparent homogeneity. The enzyme (Mr 97,000, no subunits) comprised a range of closely related molecular species ranging in isoelectric point from pH 6.6 to 7.1. Further purification to give a single protein band on isoelectric focusing (pI = 7.1) was achieved by chromatofocusing. The pH optimum of the enzyme (mixed molecular species) was 4.0-5.0 (stable from pH 3-10), and the temperature optimum was 50 degrees C (stable to 50 degrees C). It hydrolyzed lactose and beta-D-galactopyranosides but not melibiose and alpha-D-galactopyranosides. It did not release the terminal nonreducing alpha-D-galactopyranosyl residues from seed galactomannans, but catalyzed the rapid removal of terminal nonreducing beta-D-galactopyranosyl residues from xyloglucans. On the basis of the ability of the enzyme to hydrolyze xyloglucans, the kinetics of xyloglucan hydrolysis, and an experimental demonstration of a clear correlation between xyloglucan depletion and the activity in vitro of this enzyme, it is argued that the cell-wall storage xyloglucan of the nasturtium seed is its natural substrate.

Galactosidases↗
PubMed1986

Purification and properties of a novel xyloglucan-specific endo-(1----4)-beta-D-glucanase from germinated nasturtium seeds (Tropaeolum majus L.).

Endo-(1----4)-beta-D-glucanase activity has previously been detected in the cotyledons of germinated nasturtium (Tropaeolum majus L.) seeds, and has been linked to the hydrolysis in vivo of storage xyloglucan (amyloid) (Edwards, M., Dea, I. C. M., Bulpin, P. V., and Reid, J. S. G. (1985) Planta (Berl.) 163, 133-140). Extracts from the cotyledons of 14-day seedlings are now shown to contain a single endo-glucanase activity, and it has been purified to apparent homogeneity by sequential anion-exchange chromatography, cation-exchange chromatography, and gel filtration. The purified enzyme gave a single protein band on polyacrylamide gel electrophoresis, dodecyl sulfate gel electrophoresis, and isoelectric focusing. The isoelectric point was 5.0, the pH optimum 4.5-5.0, and the temperature optimum 40 degrees C. Dodecyl sulfate electrophoresis gave a molecular weight of 29,000; permeation methods gave lower values. The enzyme contained about 5% carbohydrate. An endo mode of action on tamarind seed xyloglucan was deduced by monitoring solution viscosity and reducing power, and by analyzing the end products of the reaction. The specificity of the enzyme toward a wide range of substrates, including celluloses, carboxymethyl and hydroxyethyl celluloses, glucomannan, galactoglucomannans, mixed-linkage (1----3 and 1----4)-beta-D-glucan, laminarin, and xyloglucans from seeds and primary cell walls, was tested. Only the xyloglucans were hydrolyzed. It is concluded that the enzyme is a pure, endo-acting (1----4)-beta-D-glucanase which is novel in its apparently complete specificity toward xyloglucans. It is speculated that enzymes of this type may have escaped earlier detection because it is normal practice to screen for endo-(1----4)-beta-D-glucanase using artificial cellulose derivatives and that they may be widely involved in xyloglucan metabolism in plant cell walls.

Cellulase↗
PubMed1973

Hyaluronic acid: a novel, double helical molecule.

Films prepared from a deformable gel (or putty) of hyaluronic acid show high crystallinity and orientation in their x-ray diffraction patterns. We have derived a probable structure for the molecules in these films. This is a double helix in which two identical, left-handed strands are antiparallel to one another. Each strand has four disaccharide residues per pitch length. Although the putty is prepared at pH 2.5, at which dilute solutions of hyaluronic have exaggerated rheological properties, the double helical form can also exist at physiological pH and therefore may be a biologically important form.

Circular Dichroism↗