Two-dimensional electrophoresis of 1D-encoded B and D glutenin subunits in common wheats with similar omega gliadins

1991 ◽  
Vol 29 (7-8) ◽  
pp. 403-413 ◽  
Author(s):  
S. Masci ◽  
E. Porceddu ◽  
D. Lafiandra
2013 ◽  
Vol 45 (3) ◽  
pp. 240-252 ◽  
Author(s):  
Jong-Yeol Lee ◽  
Chul-Soo Park ◽  
Hyo-Jung Kim ◽  
Joo-Hyung Kim ◽  
Min-Suk Kim ◽  
...  

1995 ◽  
Vol 16 (1) ◽  
pp. 1005-1009 ◽  
Author(s):  
Andrea Curioni ◽  
Marie-Hélène Morel ◽  
Luca Furegon ◽  
Rita Redaelli ◽  
Angelo Dal Belin Peruffo

1986 ◽  
Vol 47 (3) ◽  
pp. 175-179 ◽  
Author(s):  
Peter I. Payne ◽  
Mary S. Roberts ◽  
Linda M. Holt

SummaryOver one hundred backcross-one progeny were analysed by two dimensional electrophoresis to locate the genes on the short arm of chromosome 1D which code for, or control, the D group of LMW glutenin subunits. Recombination between these genes and Glu-D 1, encoding HMW glutenin subunits, was frequent but none could be detected between the D subunit genes and Gli-D1, coding for ω-gliadins, γ-gliadins and the B group of LMW glutenin subunits. These results are in contrast to those for chromosome 1 B because apparently homoeologous D subunit genes occur at a different position, being equidistant between Glu-B 1 (homoeologous to Glu-D 1) and Gli-B 1 (homoeologous to Gli-D 1). A range of 18 genetically-diverse wheat varieties, each containing one of two allelic groups of 1 D-encoded D subunits, were also analysed by two-dimensional electrophoresis. Consistent with the genetic analysis above, unbreakable linkages were found between these alleles and alleles of Gli-D 1. The results are discussed in relation to the evolution of the distribution of prolamin genes in the wheat genome.


1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.


2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN

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