scholarly journals Rapid and Easy High-Molecular-Weight Glutenin Subunit Identification System by Lab-on-a-Chip in Wheat (Triticum aestivum L.)

Plants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1517
Author(s):  
Dongjin Shin ◽  
Jin-Kyung Cha ◽  
So-Myeong Lee ◽  
Nkulu Rolly Kabange ◽  
Jong-Hee Lee

Lab-on-a-chip technology is an emerging and convenient system to easily and quickly separate proteins of high molecular weight. The current study established a high-molecular-weight glutenin subunit (HMW-GS) identification system using Lab-on-a-chip for three, six, and three of the allelic variations at the Glu-A1, Glu-B1, and Glu-D1 loci, respectively, which are commonly used in wheat breeding programs. The molecular weight of 1Ax1 and 1Ax2* encoded by Glu-A1 locus were of 200 kDa and 192 kDa and positioned below 1Dx subunits. The HMW-GS encoded by Glu-B1 locus were electrophoresed in the following order below 1Ax1 and 1Ax2*: 1Bx13 ≥ 1Bx7 = 1Bx7OE > 1Bx17 > 1By16 > 1By8 = 1By18 > 1By9. 1Dx2 and Dx5 showed around 4-kDa difference in their molecular weights, with 1Dy10 and 1Dy12 having 11-kDa difference, and were clearly differentiated on Lab-on-a-chip. Additionally, some of the HMW-GS, including 1By8, 1By18, and 1Dy10, having different theoretical molecular weights showed similar electrophoretic mobility patterns on Lab-on-a-chip. The relative protein amount of 1Bx7OE was two-fold higher than that of 1Bx7 or 1Dx5 and, therefore, translated a significant increase in the protein amount in 1Bx7OE. Similarly, the relative protein amounts of 8 & 10 and 10 & 18 were higher than each subunit taken alone. Therefore, this study suggests the established HMW-GS identification system using Lab-on-a-chip as a reliable approach for evaluating HMW-GS for wheat breeding programs.

2006 ◽  
Vol 57 (10) ◽  
pp. 1109 ◽  
Author(s):  
Ali-Akbar Shahnejat-Bushehri ◽  
Masoud Gomarian ◽  
Bahman Yazdi-Samadi

All current and old wheat cultivars grown in Iran were characterised by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The high-molecular-weight glutenin subunit (HMW-GS) banding patterns for each cultivar were assigned a Glu-1 quality score, a theoretical quality score based on Payne’s Glu-1 quality assignments. At the Glu-A1 loci, HMW-GS subunit compositions N, 7 + 8, 2 + 12 and 2*, 7 + 8, 2 + 12 were found to be predominant being expressed in 24 and 15 cultivars, respectively, out of 95. Eighteen different alleles were identified for the 3 loci studied: Glu-A1 (3), Glu-B1 (9), and Glu-D1 (6). The glutenin quality scores of Iranian wheat ranged from 4 to 10, with an average of 7.4. It was found that some cultivars were heterogeneous in HMW-GS composition. In cv. Cooleh, only one glutenin subunit at the Glu-B1 locus was present. HMW-GS 2*** + 12′ was found in 6 cultivars and biotypes. The results obtained here describing the allelic composition of bread wheat commonly grown in Iran may be useful in wheat breeding programs selecting for good quality parameters.


2013 ◽  
Vol 38 (7) ◽  
pp. 1205-1211
Author(s):  
Xin XU ◽  
Xiao-Jun LI ◽  
Ling-Li ZHANG ◽  
Xiu-Quan LI ◽  
Xin-Ming YANG ◽  
...  

1941 ◽  
Vol 14 (3) ◽  
pp. 580-589 ◽  
Author(s):  
G. Gee ◽  
L. R. G. Treloar

Abstract As high elasticity is a property possessed only by substances of high molecular weight, it is of interest to enquire into the relation between the elastic properties of a highly elastic material such as rubber and its molecular weight. An investigation on these lines has been made possible through the work of Bloomfield and Farmer, who have succeeded in separating natural rubber into fractions having different average molecular weights. The more important physical properties of these fractions have been examined with the object of determining which of the properties are dependent on molecular weight and which are not. Fairly extensive observations were made on the fractions from latex rubber referred to as Nos. 2, 3 and 4 by Bloomfield and Farmer, and some less extensive observations were carried out on the less oxygenated portion of fraction No. 1 obtained from crepe rubber (called hereafter 1b) . Before considering these experimental results, and their relation to the molecular weights of the fractions, it will be necessary to refer briefly to the methods used for the molecular-weight determinations, and to discuss the significance of the figures obtained.


2000 ◽  
Vol 14 (1) ◽  
pp. 69-75 ◽  
Author(s):  
G.D. Offner ◽  
R.F. Troxler

The existence of high-molecular-weight glycoproteins in saliva and salivary secretions has been recognized for nearly 30 years. These proteins, called mucins, are essential for oral health and perform many diverse functions in the oral cavity. Mucins have been intensively studied, and much has been learned about their biochemical properties and their interactions with oral micro-organisms and other salivary proteins. In the past several years, the major high-molecular-weight mucin in salivary secretions has been identified as MUC5B, one of a family of 11 human mucin gene products expressed in tissue-specific patterns in the gastrointestinal, respiratory, and reproductive tracts. MUC5B is one of four gel-forming mucins which exist as multimeric proteins with molecular weights greater than 20-40 million daltons. The heavily glycosylated mucin multimers form viscous layers which protect underlying epithelial surfaces from microbial, mechanical, and chemical assault. Another class of mucin molecules, the membrane-bound mucins, is structurally and functionally distinct from the gel-forming mucins. These proteins do not form multimers and can exist as both secreted and membrane-bound forms, with the latter anchored to epithelial cell membranes through a short membrane-spanning domain. In the present work, we show that two of the membrane-bound mucins, MUC1 and MUC4, are expressed in all major human salivary glands as well as in buccal epithelial cells. While the functions of these mucins in the oral environment are not understood, it is possible that they form a structural framework on the cell surface which not only is cytoprotective, but also may serve as a scaffold upon which MUC5B, and possibly other salivary proteins, assemble.


2004 ◽  
Vol 77 (2) ◽  
pp. 380-390
Author(s):  
Wonmun Choi ◽  
Tomoyuki Matsumura

Abstract The reactions of dichloroalkanes and sodium tetra-sulfide (Na2S4) were carried out in a mixture of water and toluene to produce corresponding cyclic polysulfides and polysulfide polymer. The low molecular weights of cyclic sulfides were obtained by the reaction at 90 °C, while the high molecular weight of polysulfide polymer was obtained by the reaction at 50 °C. GPC chromatograms and Mass spectra revealed that the structures of cyclic polysulfide were 1:1, 2:2, and 3:3 adducts of dichloroalkane and sodium tetra-sulfide. The mechanical properties of vulcanized NR at 148 °C with cyclic sulfides were similar to that with sulfur. However, both tensile strength and elongation at break of vulcanized NR at 170 °C with cyclic sulfides are much higher than that with sulfur. The aging properties of vulcanized NR at 148 °C or 170 °C with cyclic polysulfides indicate better stability.


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