scholarly journals Biosynthesis of arabinogalactan-protein in Lolium multiflorum (Italian ryegrass) endosperm cells. Subcellular distribution of galactosyltransferases

1984 ◽  
Vol 218 (2) ◽  
pp. 633-636 ◽  
Author(s):  
A Schibeci ◽  
A Pnjak ◽  
G B Fincher
Keyword(s):  
Golgi Apparatus ◽  
Subcellular Distribution ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Arabinogalactan Protein ◽  
Enzyme Assays ◽  
Marker Enzyme ◽  
Carbohydrate Component ◽  
Myeloma Protein ◽  
Putative Marker

Intracellular membranes from protoplasts of Italian-ryegrass (Lolium multiflorum) endosperm cells have been fractionated on sucrose density gradients and identified on the basis of putative-marker-enzyme assays. Galactosyltransferases capable of incorporating galactose from UDP galactose into 66% ethanol-soluble products are associated with all membrane fractions. Affinity chromatography of the ethanol-insoluble products on (murine myeloma protein J539)-Sepharose reveals that the enzymes responsible for the synthesis of polymers containing (1→6)-beta-D-galactose residues are associated exclusively with subcellular fractions enriched in Golgi-derived membranes. This suggests that the Golgi apparatus plays an important part in the synthesis of the carbohydrate component of the ryegrass arabinogalactan-protein.

scholarly journals Characterization of the hydroxyproline-rich protein core of an arabinogalactan-protein secreted from suspension-cultured Lolium multiflorum (Italian ryegrass) endosperm cells

1989 ◽  
Vol 264 (3) ◽  
pp. 857-862 ◽  
Author(s):  
P A Gleeson ◽  
M McNamara ◽  
R E H Wettenhall ◽  
B A Stone ◽  
G B Fincher
Keyword(s):  
Polyclonal Antibodies ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Arabinogalactan Protein ◽  
Myeloma Protein ◽  
Protein Core ◽  
Liquid Suspension ◽  
Peptide Component ◽  
Immunodominant Epitopes

An arabinogalactan-protein (AGP) purified from the filtrate of liquid-suspension-cultured Italian-ryegrass (Lolium multiflorum) endosperm cells by affinity chromatography on myeloma protein J539-Sepharose was deglycosylated with trifluoromethanesulphonic acid to remove polysaccharide chains that are covalently associated with hydroxyproline residues in the peptide component of the proteoglycan. The protein core, which accounts for less than 10% (w/w) of the intact proteoglycan, was purified by h.p.l.c. It has an apparent Mr of 35,000, but reacts very poorly with both Coomassie Brilliant Blue R and silver stains. Amino-acid-sequence analysis of the N-terminus of the h.p.l.c.-purified protein core and of tryptic peptides generated from the unpurified protein reveals a high content of hydroxyproline and alanine. These are sometimes arranged in short (Ala-Hyp) repeat sequences of up to six residues. Polyclonal antibodies raised against the protein core do not cross-react with native AGP, the synthetic peptide (Ala-Hyp)4, poly-L-hydroxyproline or poly-L-proline. The results suggest that the polysaccharide chains in the native AGP render the protein core of the proteoglycan inaccessible to the antibodies and that the immunodominant epitopes include domains of the protein other than those rich in Ala-Hyp repeating units.

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 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.

Inhibitory effects of Italian ryegrass (Lolium multiflorum Lam.) seedlings of rice (Oryza sativa L.)

2018 ◽  
Vol 44 (2) ◽  
pp. 219-232 ◽  
Author(s):  
S.J Jang ◽  
K.R. Kim ◽  
Y.B. Yun ◽  
S.S. Kim ◽  
Y.I Kuk
Keyword(s):  
Oryza Sativa ◽  
Oryza Sativa L ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Inhibitory Effects

scholarly journals Hepatic endosome fractions contain an ATP-driven proton pump

1985 ◽  
Vol 225 (1) ◽  
pp. 51-58 ◽  
Author(s):  
T Saermark ◽  
N Flint ◽  
W H Evans
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Atpase Activity ◽  
Proton Pump ◽  
Subcellular Distribution ◽  
Plasma Membranes ◽  
Specific Activity ◽  
Ph Gradients ◽  
Subcellular Organelle ◽  
Liver Homogenates

Endosome fractions were isolated from rat liver homogenates on the basis of the subcellular distribution of circulating ligands, e.g. 125I-asialotransferrin internalized by hepatocytes by a receptor-mediated process. The distribution of endocytosed 125I-asialotransferrin 1-2 min and 15 min after uptake by liver and a monensin-activated Mg2+-dependent ATPase activity coincided on linear gradients of sucrose and Nycodenz. The monensin-activated Mg2+-ATPase was enriched relative to the liver homogenates up to 60-fold in specific activity in the endosome fractions. Contamination of the endosome fractions by lysosomes, endoplasmic reticulum, mitochondria, plasma membranes and Golgi-apparatus components was low. By use of 9-aminoacridine, a probe for pH gradients, the endosome vesicles were shown to acidify on addition of ATP. Acidification was reversed by addition of monensin. The results indicate that endosome fractions contain an ATP-driven proton pump. The ionophore-activated Mg2+-ATPase in combination with the presence of undegraded ligands in the endosome fractions emerge as linked markers for this new subcellular organelle.

Quantitative trait loci analysis of nitrate-nitrogen content in Italian ryegrass (Lolium multiflorum Lam.)

Euphytica ◽  
2021 ◽  
Vol 217 (1) ◽  
Author(s):  
Wenqing Tan ◽  
Di Zhang ◽  
Nana Yuyama ◽  
Jun Chen ◽  
Shinichi Sugita ◽  
...  
Keyword(s):  
Quantitative Trait Loci ◽  
Nitrogen Content ◽  
Quantitative Trait ◽  
Nitrate Nitrogen ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Trait Loci

Protection of Italian ryegrass (Lolium multiflorum L.) seedlings from salinity stress following seed priming with L-methionine and casein hydrolysate

2020 ◽  
pp. 1-9
Author(s):  
Keum-Ah Lee ◽  
Youngnam Kim ◽  
Hossein Alizadeh ◽  
David W.M. Leung
Keyword(s):  
Oxidative Stress ◽  
Amino Acids ◽  
Salinity Stress ◽  
Lolium Multiflorum ◽  
Casein Hydrolysate ◽  
Seed Priming ◽  
Germination Percentage ◽  
Italian Ryegrass ◽  
Significant Difference ◽  
Protein Amino Acids

Abstract Seed priming with water (hydropriming or HP) has been shown to be beneficial for seed germination and plant growth. However, there is little information on the effects of seed priming with amino acids and casein hydrolysate (CH) compared with HP, particularly in relation to early post-germinative seedling growth under salinity stress. In this study, Italian ryegrass seeds (Lolium multiflorum L.) were primed with 1 mM of each of the 20 protein amino acids and CH (200 mg l−1) before they were germinated in 0, 60 and 90 mM NaCl in Petri dishes for 4 d in darkness. Germination percentage (GP), radicle length (RL) and peroxidase (POD) activity in the root of 4-d-old Italian ryegrass seedlings were investigated. Generally, when the seeds were germinated in 0, 60 and 90 mM NaCl, there was no significant difference in GP of seeds among various priming treatments, except that a higher GP was observed in seeds of HP treatment compared with the non-primed seeds when incubated in 60 mM NaCl. When incubated in 60 and 90 mM NaCl, seedlings from seeds primed with L-methionine or CH exhibited greater RL (greater protection against salinity stress) and higher root POD activity than those from non-primed and hydro-primed seeds. Under salinity stress, there were higher levels of malondialdehyde (MDA) in the root of 4-d-old Italian ryegrass seedlings, a marker of oxidative stress, but seed priming with CH was effective in reducing the salinity-triggered increase in MDA content. These results suggest that priming with L-methionine or CH would be better than HP for the protection of seedling root growth under salinity stress and might be associated with enhanced antioxidative defence against salinity-induced oxidative stress.

Seed germination behavior of glyphosate‐resistant and susceptible Italian ryegrass ( Lolium multiflorum Lam.)

2020 ◽  
Author(s):  
Afonso Henrique Schaeffer ◽  
Diógenes Cecchin Silveira ◽  
Otávio Augusto Schaeffer ◽  
Nadia Canali Lângaro ◽  
Leandro Vargas
Keyword(s):  
Seed Germination ◽  
Lolium Multiflorum ◽  
Italian Ryegrass
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