scholarly journals Molecular Cloning of a β-Galactosidase from Radish That Specifically Hydrolyzes β-(1→3)- and β-(1→6)-Galactosyl Residues of Arabinogalactan Protein

2005 ◽  
Vol 138 (3) ◽  
pp. 1563-1576 ◽  
Author(s):  
Toshihisa Kotake ◽  
Soraya Dina ◽  
Tomoyuki Konishi ◽  
Satoshi Kaneko ◽  
Kiyohiko Igarashi ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Arabinogalactan Protein ◽  
Galactosyl Residues

Biosynthesis of Arabinogalactan-Protein in Lolium multiflorum (Ryegrass) Endosperm Cells. II. In vitro Incorporation of Galactosyl Residues From UDPgalactose Into Polymeric Products

1982 ◽  
Vol 9 (1) ◽  
pp. 31 ◽  
Author(s):  
T Mascara ◽  
GB Fincher
Keyword(s):  
Cell Walls ◽  
Membrane Fraction ◽  
Lolium Multiflorum ◽  
Apparent Molecular Weight ◽  
Arabinogalactan Protein ◽  
Methylation Data ◽  
Myeloma Protein ◽  
Mouse Myeloma ◽  
Galactosyl Residues

When mixed-membrane fractions from suspension-cultured Lolium multiflorum endosperm cells are incubated in vitro with UDP-[14C]galactose, 66% ethanol-insoluble products of apparent molecular weight greater than 60 000 are labelled in both galactosyl and glucosyl residues, suggesting that an active UDPgalactose 4-epimerase is present on the membrane fraction. The epimerase can be inhibited with ADPribose, to produce polymeric material in which [14C]galactosyl residues pre-dominate. While some of these residues appear to be associated with glycoproteins, affinity chromatography of the products on mouse myeloma protein J539-Sepharose provides evidence that β-galactans containing 1,6-linkages are amongst the products. Monosaccharide analyses and methylation data indicate that the mixed-membrane preparations contain associated polysaccharide of structure analogous to the 1,3;1,4-β-glucans, arabinoxylans and arabino-3,6-galactans normally found in cell walls or secreted into the medium.

scholarly journals Antigenic determinants of a plant proteoglycan, the Gladiolus style arabinogalactan-protein

1980 ◽  
Vol 191 (2) ◽  
pp. 437-447 ◽  
Author(s):  
P A Gleeson ◽  
A E Clarke
Keyword(s):  
Potent Inhibitor ◽  
Cross Reactivity ◽  
Arabinogalactan Protein ◽  
Galactose Oxidase ◽  
Antigenic Specificity ◽  
Specific Antiserum ◽  
Antigenic Determinants ◽  
Carbohydrate Component ◽  
Terminal Galactose ◽  
Galactosyl Residues

Antiserum has been raised to the arabinogalactan-protein of Gladiolus style mucilage. This macromolecule has been characterized and has a structure consistent with a 1 leads to 3-linked beta-galactan backbone with side branches of 1 leads to 6-linked beta-galactosyl residues, some of which carry terminal alpha-L-arabinofuranoside residues [Gleeson & Clarke (1979) Biochem. J. 181, 607-621]. The specificity of the antiserum has been investigated by immunoprecipitation with [3H]arabinogalactan-protein. THe 3H label was introduced into the arabinogalactan-protein by oxidation of the terminal galactose residues with galactose oxidase, followed by reduction with NaB3H4. The antigenic specificity of the antiserum was shown to be directed towards the carbohydrate component of the arabinogalactan-protein. D-galactose and L-arabinose were the most effective hapten inhibitors of the antiserum; other monosaccharides, N-acetyl-D-galactono-1,4-lactone, D-glucose, D-mannose, L-rhamnose. L-fucose and D-xylose, were all poor inhibitors. The antiserum showed preference for beta-galactosides over alpha-galactosides. Of the haptens examined, the disaccharide 6-O-beta-D-galactopyranosyl-D-galactopyranose was the most potent inhibitor. The antigenic features of the arabinogalactan-protein were investigated by examining the interaction of the antiserum with chemically and enzymically modified arabinogalactan-protein. Also, the cross-reactivity of structurally related polysaccharides and glycoproteins with the specific antiserum was assessed by a haemagglutination assay using erythrocytes coupled with specific antiserum. The results indicate that the dominant antigenic determinants of the arabinogalactan-protein are probably the side branches of 1 leads to 6 -linked beta-galactose residues bearing the terminal alpha-L-arabinose residues.

scholarly journals Reaction of Some Invertebrate and Plant Agglutinins and a Mouse Myeloma Anti-Galactan Protein With an Arabinogalactan From Wheat

1978 ◽  
Vol 31 (2) ◽  
pp. 149 ◽  
Author(s):  
BA Baldo ◽  
H Neukom ◽  
BA Stone ◽  
G Uhlenbruck
Keyword(s):  
Ricinus Communis ◽  
Lolium Multiflorum ◽  
Arabinogalactan Protein ◽  
Myeloma Protein ◽  
Tridacna Maxima ◽  
The Difference ◽  
Inhibition Studies ◽  
Mild Acid ◽  
Mouse Myeloma ◽  
Galactosyl Residues

Plant, invertebrate and vertebrate proteins which show anti-galactan combining specificities were used in precipitation and inhibition studies with arabinogalactan preparations from wheat and ryegrass (Lolium multiflorum). Of the agglutinins studied, only mouse anti-galactan myeloma protein J539 showed strong reactivity with wheat arabinoglactan-peptide. Weak reactions were observed with the agglutinins from the clam Tridacna maxima, the sponge Axinella polypoides and the anemone Cerianthus membranaceus. No reactions were detected with lectins from the plants Abrus precatorius and Ricinus communis. Reactions readily occurred between Lolium arabinogalactan-protein and the invertebrate and vertebrate agglutinins. Removal of terminal arabinosyl residues from the wheat and Lotium arabinogalactans either by mild acid hydrolysis or by treatment with an arabinofuranosidase increased the reactivity of both peptidoglycans with all of the agglutinins examined except the Ricinus RCAl lectin. Results obtained with wheat arabinogalactan indicate that few D-galactose units are terminal and available for reaction. The difference in reactivities between the wheat and Lotium arabinogalactans may be due to the differences in the galactose:arabinose ratios or to differences in linkage of the galactosyl residues on the two peptidoglycans, or both. Results indicate that the mouse anti-galactan could be a useful reagent for the subcellular localization of wheat arabinogalactan and that tridacnin and Axinella agglutinins could be used to localize the arabinogalactan in L. multiflorum cells.

Molecular cloning and characterization of vernalization-related (ver) genes in winter wheat

1994 ◽  
Vol 92 (3) ◽  
pp. 511-515 ◽  
Author(s):  
Kang Chong ◽  
Li-Ping Wang ◽  
Ke-Hui Tan ◽  
Hua-Liang Huang ◽  
Hou-Guo Liang
Keyword(s):  
Winter Wheat ◽  
Molecular Cloning

The molecular cloning of dihydroartemisinic aldehyde reductase and its implication in artemisinin biosynthesis in Artemisia annua

Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
O Kayser ◽  
A Ryden ◽  
H Bouwmeester ◽  
C Ruyter Spira ◽  
H Osada ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Artemisia Annua ◽  
Aldehyde Reductase ◽  
Artemisinin Biosynthesis
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