Immunocytochemical localization of wheat prolamins in the lumen of the rough endoplasmic reticulum

1991 ◽  
Vol 69 (11) ◽  
pp. 2574-2577 ◽  
Author(s):  
Hari B. Krishnan ◽  
Jerry A. White ◽  
Steven G. Pueppke
Keyword(s):  
Triticum Aestivum ◽  
Endoplasmic Reticulum ◽  
Key Words ◽  
Rough Endoplasmic Reticulum ◽  
Protein A ◽  
Triticum Aestivum L ◽  
Soluble Proteins ◽  
Immunocytochemical Localization ◽  
Specific Antibodies ◽  
Days After Anthesis

Antibodies raised against gliadins, the alcohol-soluble proteins of wheat (Triticum aestivum L.) seeds, were used to localize gliadins within the lumen of the endoplasmic reticulum. Endosperm cells at 20 days after anthesis contain extensive rough endoplasmic reticulum that is fragmented and dilated. The dilated endoplasmic reticulum encloses aggregates of proteinaceous material that reacts strongly with gliadin-specific antibodies. Key words: gliadins, immunocytochemistry, protein A – gold, rough endoplasmic reticulum, wheat.

Etude des protéines des blés résistant, Kharkov, et sensible, Selkirk, au cours de l'endurcissement au froid. I. Protéines solubles

1975 ◽  
Vol 53 (21) ◽  
pp. 2411-2416 ◽  
Author(s):  
E. Rochat ◽  
H. P. Therrien
Keyword(s):  
Amino Acids ◽  
Triticum Aestivum ◽  
Triticum Aestivum L ◽  
Soluble Proteins ◽  
Cold Hardening ◽  
Ice Formation

Electrophoregrams of soluble proteins of winter wheats (Triticum aestivum L.) after incorporation of L-[14C] leucine disclose the synthesis of two particular proteins during the cold hardening processes of the hardier variety, Kharkov, compared with a less-hardy variety, Selkirk. The composition in amino acids of the two proteins has been studied and shown to confer them a higher degree of hydrophily making them capable to bind and retain vital water with enough energy to avoid too much dehydration resulting in denaturation during extracellular ice formation.

Chromosome localization of genes for soluble proteins in hexaploid wheat (triticum aestivum L.)

1991 ◽  
Vol 33 (2) ◽  
pp. 145-149
Author(s):  
Ts. Stoilova ◽  
G. Ganeva ◽  
B. Bochev ◽  
K. Petkolicheva
Keyword(s):  
Triticum Aestivum ◽  
Hexaploid Wheat ◽  
Triticum Aestivum L ◽  
Soluble Proteins ◽  
Chromosome Localization

scholarly journals Immunocytochemical localization of procollagen and fibronectin in human fibroblasts: effects of the monovalent ionophore, monensin.

1980 ◽  
Vol 87 (3) ◽  
pp. 663-671 ◽  
Author(s):  
P W Ledger ◽  
N Uchida ◽  
M L Tanzer
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Immunofluorescence Microscopy ◽  
Human Fibroblasts ◽  
Subsequent Development ◽  
Immunocytochemical Localization ◽  
Intracellular Accumulation ◽  
Golgi Compartment ◽  
Golgi Zone ◽  
Ionophore Monensin

The monovalent ionophore monensin inhibits the secretion of both procollagen and fibronectin from human fibroblasts in culture. The distribution of these proteins in control and inhibited (5 x 10(-7) M monensin) cells has been studied by immunofluorescence microscopy. In control cells, both antigens are present throughout the cytoplasm and in specific deposits in a region adjacent to the nucleus, which we identify as a Golgi zone by electron microscopy. Treatment of cells with monensin causes intracellular accumulation of procollagen and fibronectin, initially in the juxta-nuclear region and also subsequently in peripheral regions. Electron microscope studies reveal that in such cells the juxta-nuclear Golgi zone becomes filled with a new population of smooth-membraned vacuoles and that normal Golgi complexes are not found. Immunocytochemically detected procollagen and fibronectin are localized in the region of these vacuoles, whereas more peripheral deposits correspond to the dilated cisternae of rough endoplasmic reticulum, which are also caused by monensin. Procollagen and fibronectin are often codistributed in these peripheral deposits. Accumulation of exportable proteins in Golgi-related vacuoles is consistent with previous analyses of the monensin effect. The subsequent development of dilated rough endoplasmic reticulum also containing accumulated proteins may indicate that there is an additional blockade at the exit from the endoplasmic reticulum, or that the synthesized proteins exceed the capacity of the Golgi compartment and that their accumulation extends into the endoplasmic reticulum.

Response to weed control by four spring wheat genotypes differing in competitive ability

1998 ◽  
Vol 78 (1) ◽  
pp. 171-173 ◽  
Author(s):  
P. Hucl
Keyword(s):  
Triticum Aestivum ◽  
Grain Yield ◽  
Key Words ◽  
Weed Control ◽  
Spring Wheat ◽  
Competitive Ability ◽  
Triticum Aestivum L ◽  
Control Methods ◽  
Wheat Genotypes ◽  
Control Genotype

Increased crop competitiveness may complement existing weed control methods. The objective of this research was to establish whether spring wheat (Triticum aestivum L.) genotypes with contrasting competitive abilities respond differently to weed control levels. Four sibling genotypes differing in competitive ability were grown under simulated weedy conditions and subjected to four weed control levels. The competitive genotypes were superior to the less-competitive genotypes in grain yield under weedy and partially weedy conditions. Key words: Triticum aestivum L., competition, weed control, genotype × weedcontrol interaction

Chromosome location and linkage of a new gene (Lr33) for reaction to Puccinia recondita in common wheat

Genome ◽  
1987 ◽  
Vol 29 (3) ◽  
pp. 463-466 ◽  
Author(s):  
P. L. Dyck ◽  
E. R. Kerber ◽  
O. M. Lukow
Keyword(s):  
Triticum Aestivum ◽  
Key Words ◽  
Common Wheat ◽  
Triticum Aestivum L ◽  
Translocation Breakpoint ◽  
Puccinia Recondita ◽  
Chromosome Location ◽  
Backcross Line ◽  
New Gene ◽  
Recombination Value

A gene for resistance to Puccinia recondita, originally detected in wheat (Triticum aestivum L.) accessions PI58548, PI268454, and PI268316, has been located on the long arm of chromosome 1B, 3.1 ± 1.2 crossover units from the centromere. In a cross between the backcross line RL6057 containing this new gene, now designated Lr33, and the backcross line RL6078 containing gene Lr26, gene Lr33 is closely linked to gene Lr26 (or the translocation breakpoint) with an estimated 2.6 ± 0.8 recombination value. RL6057 and RL6078 differ in gliadin bands that are controlled by genes on the short arm of chromosome 1B or 1R. The banding difference was completely associated with the presence or absence of Lr26. Key words: Triticum, Puccinia, linkage.

scholarly journals Proteoglycan biosynthesis in chondrocytes: protein A-gold localization of proteoglycan protein core and chondroitin sulfate within Golgi subcompartments.

1985 ◽  
Vol 101 (6) ◽  
pp. 2355-2365 ◽  
Author(s):  
A Ratcliffe ◽  
P R Fryer ◽  
T E Hardingham
Keyword(s):  
Endoplasmic Reticulum ◽  
Chondroitin Sulfate ◽  
Rough Endoplasmic Reticulum ◽  
Intracellular Localization ◽  
Protein A ◽  
Keratan Sulfate ◽  
Glycosaminoglycan Synthesis ◽  
Protein Core ◽  
Late Event ◽  
Secretory Glycoproteins

The intracellular pathway of cartilage proteoglycan biosynthesis was investigated in isolated chondrocytes using a protein A-gold electron microscopy immunolocalization procedure. Proteoglycans contain a protein core to which chondroitin sulfate and keratan sulfate chains and oligosaccharides are added in posttranslational processing. Specific antibodies have been used in this study to determine separately the distribution of the protein core and chondroitin sulfate components. In normal chondrocytes, proteoglycan protein core was readily localized only in smooth-membraned vesicles which co-labeled with ricin, indicating them to be galactose-rich medial/trans-Golgi cisternae, whereas there was only a low level of labeling in the rough endoplasmic reticulum. Chondroitin sulfate was also localized in medial/trans-Golgi cisternae of control chondrocytes but was not detected in other cellular compartments. In cells treated with monensin (up to 1.0 microM), which strongly inhibits proteoglycan secretion (Burditt, L.J., A. Ratcliffe, P. R. Fryer, and T. Hardingham, 1985, Biochim. Biophys. Acta., 844:247-255), there was greatly increased intracellular localization of proteoglycan protein core in both ricin-positive vesicles, and in ricin-negative vesicles (derived from cis-Golgi stacks) and in the distended rough endoplasmic reticulum. Chondroitin sulfate also increased in abundance after monensin treatment, but continued to be localized only in ricin-positive vesicles. The results suggested that the synthesis of chondroitin sulfate on proteoglycan only occurs in medial/trans-Golgi cisternae as a late event in proteoglycan biosynthesis. This also suggests that glycosaminoglycan synthesis on proteoglycans takes place in a compartment in common with events in the biosynthesis of both O-linked and N-linked oligosaccharides on other secretory glycoproteins.

Harmil winter wheat

1991 ◽  
Vol 71 (2) ◽  
pp. 543-546
Author(s):  
D. R. Sampson ◽  
R. G. Fulcher ◽  
W. L. Seaman ◽  
J. Fregeau-Reid
Keyword(s):  
Triticum Aestivum ◽  
Winter Wheat ◽  
Key Words ◽  
Triticum Aestivum L ◽  
High Yield ◽  
Loose Smut ◽  
Ustilago Tritici ◽  
Flour Protein ◽  
Cultivar Description ◽  
1000 Grain Weight

Harmil is a new soft white winter wheat (Triticum aestivum L.) cultivar well adapted to southwestern Ontario. It has high yield, medium height, strong straw, low grain and flour protein, and low 1000-grain weight. It is moderately susceptible to leaf and head diseases, but it is the only cultivar available for the area that is resistant to the two prevalent races of loose smut (Ustilago tritici). Key words: Triticum aestivum L., wheat (winter), soft white, cultivar description

Inheritance of kernel hardness in five spring wheat crosses

1991 ◽  
Vol 71 (1) ◽  
pp. 179-181 ◽  
Author(s):  
R. J. Baker ◽  
K. A. Sutherland
Keyword(s):  
Triticum Aestivum ◽  
Key Words ◽  
Spring Wheat ◽  
Significant Variation ◽  
Triticum Aestivum L ◽  
Genetic Differences ◽  
Kernel Hardness ◽  
Grinding Time

Significant variation among grinding times of F3-derived F4 lines of five crosses indicated that there were genetic differences in hardness among five spring wheat (Triticum aestivum L.) cultivars. Bimodal distributions indicated a two-gene difference between a very hard and soft cultivar and a one-gene difference between a hard and soft cultivar. Key words: Triticum aestivum, kernel hardness, grinding time

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