scholarly journals Characterization of Pakistani wheat germplasm for high and low molecular weight glutenin subunits using SDS-PAGE

2019 ◽  
pp. 1-11
Author(s):  
A. Khalid ◽  
A. Hameed
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Wheat Germplasm ◽  
Sds Page

Characterization of CIMMYT bread wheats for high- and low-molecular weight glutenin subunits and other quality-related genes with SDS-PAGE, RP-HPLC and molecular markers

Euphytica ◽  
2009 ◽  
Vol 172 (2) ◽  
pp. 235-250 ◽  
Author(s):  
Dan Liang ◽  
Jianwei Tang ◽  
Roberto Javier Peña ◽  
Ravi Singh ◽  
Xinyao He ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Molecular Markers ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Rp Hplc ◽  
Sds Page

Characterization of a wheat mutant missing low-molecular-weight glutenin subunits encoded by the B-genome

2017 ◽  
Vol 73 ◽  
pp. 158-164 ◽  
Author(s):  
Jong-Yeol Lee ◽  
Chon-Sik Kang ◽  
Hye-Rang Beom ◽  
You-Ran Jang ◽  
Susan B. Altenbach ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
B Genome ◽  
Wheat Mutant

Rapid Characterization of Wheat Low Molecular Weight Glutenin Subunits by Ultraperformance Liquid Chromatography (UPLC)

2013 ◽  
Vol 61 (17) ◽  
pp. 4026-4034 ◽  
Author(s):  
Zitong Yu ◽  
Caixia Han ◽  
Xing Yan ◽  
Xiaohui Li ◽  
Guoliang Jiang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Liquid Chromatography ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Rapid Characterization

scholarly journals Cloning and Characterization of Low-Molecular-Weight Glutenin Subunit Alleles from Chinese Wheat Landraces (Triticum aestivumL.)

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Hongqi Si ◽  
Manli Zhao ◽  
Xin Zhang ◽  
Guoliang Yao ◽  
Genlou Sun ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Disulfide Bonds ◽  
Low Molecular Weight ◽  
Processing Quality ◽  
Repetitive Domain ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Wheat Landraces ◽  
Chinese Wheat

Low-molecular-weight glutenin subunits (LMW-GS) are of great importance in processing quality and participate in the formation of polymers in wheat. In this study, eight new LMW-GS alleles were isolated from Chinese wheat landraces (Triticum aestivumL.) and designated asGlu-A3-1a,Glu-A3-1b,Glu-B3-1a,Glu-B3-1b,Glu-B3-1c,Glu-D3-1a,Glu-D3-1b, andGlu-D3-1c, which were located at theGlu-A3,Glu-B3, andGlu-D3loci, respectively. Based on the proteins encoded, the number of deduced amino acids ofGlu-B3alleles was approximately 50 more than those ofGlu-A3andGlu-D3alleles. The first cysteine ofGlu-A3andGlu-D3alleles was located at the N-terminal domain, while that ofGlu-B3alleles was found in the repetitive domain, which may lead to the different functioning in forming disulfide bonds. All the eight genes were LMW-m types and the new allele ofGlu-B3-1awhich had nine cysteine residues may be the desirable LMW-GS gene for improving bread-making quality.

scholarly journals Purification and characterization of a low molecular weight xylanase from solid-state cultures of Aspergillus fumigatus Fresenius

1999 ◽  
Vol 30 (2) ◽  
pp. 114-119 ◽  
Author(s):  
Claudio Henrique Cerri e Silva ◽  
Jurgen Puls ◽  
Marcelo Valle de Sousa ◽  
Edivaldo Ximenes Ferreira Filho
Keyword(s):  
Molecular Weight ◽  
Solid State ◽  
Aspergillus Fumigatus ◽  
Gel Filtration ◽  
Low Molecular Weight ◽  
Transferase Activity ◽  
Purification And Characterization ◽  
Apparent Homogeneity ◽  
Sds Page

A xylan-degrading enzyme (xylanase II) was purified to apparent homogeneity from solid-state cultures of Aspergillus fumigatus Fresenius. The molecular weight of xylanase II was found to be 19 and 8.5 kDa, as estimated by SDS-PAGE and gel filtration on FPLC, respectively. The purified enzyme was most active at 55 °C and pH 5.5. It was specific to xylan. The apparent Km and Vmax values on soluble and insoluble xylans from oat spelt and birchwood showed that xylanase II was most active on soluble birchwood xylan. Studies on hydrolysis products of various xylans and xylooligomers by xylanase II on HPLC showed that the enzyme released a range of products from xylobiose to xylohexaose, with a small amount of xylose from xylooligomers, and presented transferase activity.

Mass Spectrometric Approaches for the Characterization of Low-Molecular Weight Glutenin Subunits

2011 ◽  
pp. 34-37 ◽  
Author(s):  
V. Cunsolo ◽  
S. Foti ◽  
V. Muccilli ◽  
R. Saletti ◽  
D. Lafiandra ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Mass Spectrometric ◽  
Low Molecular Weight ◽  
Glutenin Subunits
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