scholarly journals Isolation and identification of mRNA for the high-molecular-weight storage proteins of wheat endosperm

Planta ◽  
1983 ◽  
Vol 157 (6) ◽  
pp. 567-576 ◽  
Author(s):  
J. Forde ◽  
B. J. Miflin
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Isolation And Identification ◽  
Wheat Endosperm

Isolation and identification of an α2 subclass lymphotoxin (LT) subunit from the high-molecular-weight (complex) human LT class

1984 ◽  
Vol 88 (2) ◽  
pp. 297-308 ◽  
Author(s):  
James J. Devlin ◽  
Jim Klostergaard ◽  
Gale A. Granger
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Isolation And Identification ◽  
High Molecular Weight Complex

The high-molecular-weight glutenin subunit composition of Japanese hexaploid wheat landraces

2000 ◽  
Vol 51 (6) ◽  
pp. 673 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Storage Proteins ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Landraces

The endosperm storage proteins of 174 Japanese wheat (Triticum aestivum) landraces were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine their high-molecular-weight (HMW) glutenin subunit composition. These are alleles for complex gene loci, Glu-A1, Glu-B1, and Glu-D1, that are present in Japanese hexaploid wheat landraces. These were identified by comparison with the subunit mobility previously found in hexaploid wheat. Twenty-four different, major glutenin HMW subunits were identified. Each landrace contained 3–5 subunits, and 17 different glutenin subunit patterns were observed for 13 alleles in Japanese landraces. Japanese landraces showed specific allelic variation in glutenin HMW subunits, different from those in non-Japanese hexaploid wheats.

scholarly journals The composition of gluten proteins and their effect on the rheological properties of gluten

2006 ◽  
pp. 124-129
Author(s):  
Csilla Uri ◽  
Árpád Tóth ◽  
Péter Sipos ◽  
Mária Borbélyné Varga ◽  
Zoltán Győri
Keyword(s):  
Molecular Weight ◽  
Rheological Properties ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Wheat Varieties ◽  
Gluten Proteins ◽  
Two Factors ◽  
Protein Components

Wheat is the major cereal component of bread in the world and is grown worldwide. Of the cereals only the bread wheats – and less the triticale – includes storage proteins that play an important role in the performance of gluten. Proteins of gluten complex may be present in two classes:− low molecular weight (gliadin-) components, and− high molecular weight (glutenin-) components.Gliadins shown appreciable heterogenity and can be separated into 40-50 components with gel electrophoresis. The composition of gliadins is employable for the identification the wheat varieties and to investigate the varieties. In the decreasing electrophoretic mobility sequence may be distinguish α-, β-, γ- and ω-gliadins. A glutenin subunits may be include in two classes:− high molecular weight glutenin subunits (HMW-GS),− low molecular weight glutenin subunits (LMW-GS).Wheat varieties can be identified by glutenin and their quality selection is also possible. The gliadin’s polypeptides encoding genes are located on the short arm of chromosomes 1A, 1B and 1D, 6A, 6B and 6D. Genetic coding for HMW subunits is located on the long arms of chromosomes 1A, 1B and 1D, the LMW-GS are also located on chromosomes 1A, 1B and 1D (Glu-3 loci) near the gliadin-coding loci.Storage proteins affect the rheological properties of gluten by two factors:1. The quality and quantity of the protein components of the gluten complex,2. The interactions between the protein fractions.

An approach for isolating high-molecular-weight glutenin subunit genes using monoclonal antibodies

Genome ◽  
2006 ◽  
Vol 49 (2) ◽  
pp. 181-189 ◽  
Author(s):  
H Q Wang ◽  
X Y Zhang
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Sds Page

High-molecular-weight glutenin subunits (HMW-GSs) play an important role in the breadmaking quality of wheat flour. In China, cultivars such as Triticum aestivum 'Xiaoyan No. 6' carrying the 1Bx14 and 1By15 glutenin subunits usually have attributes that result in high-quality bread and noodles. HMW-GS 1Bx14 and 1By15 were isolated by preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and used as an antigen to immunize BALB/c mice. A resulting monoclonal antibody belonging to the IgG1 subclass was shown to bind to all HMW-GSs of Triticum aestivum cultivars, but did not bind to other storage proteins of wheat seeds in a Western blot analysis. After screening a complementary DNA expression library from immature seeds of 'Xiaoyan No. 6' using the monoclonal antibody, the HMW-GS 1By15 gene was isolated and fully sequenced. The deduced amino acid sequence showed an extra stretch of 15 amino acid repeats consisting of a hexapeptide and a nonapeptide in the repetitive domain of this y-type HMW subunit. Bacterial expression of a modified 1By15 gene, in which the coding sequence for the signal peptide was removed and a BamHI site eliminated, gave rise to a protein with mobility identical to that of HMW-GSs extracted from seeds of 'Xiaoyan No. 6' via SDS-PAGE. This approach for isolating genes using specific monoclonal antibody against HMW-GS genes is a good alternative to the extensively used polymerase chain reaction (PCR) technology based on sequence homology of HMW-GSs in wheat and its relatives.Key words: wheat, HMW-GS, monoclonal antibody, immunoscreen.

scholarly journals Isolation and identification of a high molecular weight protein in sow milk

animal ◽  
2015 ◽  
Vol 9 (5) ◽  
pp. 847-854 ◽  
Author(s):  
Y. Qin ◽  
N. Qi ◽  
Y. Tang ◽  
J. He ◽  
X. Li ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Molecular Weight Protein ◽  
High Molecular Weight Protein ◽  
Isolation And Identification ◽  
Weight Protein

Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin

1999 ◽  
Vol 1430 (2) ◽  
pp. 359-366 ◽  
Author(s):  
Neil H. Thomson ◽  
Mervyn J. Miles ◽  
Yves Popineau ◽  
John Harries ◽  
Peter Shewry ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Small Angle ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Wheat Seed ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering
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