Characterisation of high molecular weight gliadin and low-molecular-weight glutenin subunits of wheat endosperm by two-dimensional electrophoresis and the chromosomal localisation of their controlling genes

1983 ◽  
Vol 66 (1) ◽  
pp. 29-37 ◽  
Author(s):  
E. A. Jackson ◽  
L. M. Holt ◽  
P. I. Payne
2013 ◽  
Vol 45 (3) ◽  
pp. 240-252 ◽  
Author(s):  
Jong-Yeol Lee ◽  
Chul-Soo Park ◽  
Hyo-Jung Kim ◽  
Joo-Hyung Kim ◽  
Min-Suk Kim ◽  
...  

2006 ◽  
Vol 351 (2) ◽  
pp. 290-297 ◽  
Author(s):  
Kazumi Kitta ◽  
Mayumi Ohnishi-Kameyama ◽  
Tatsuya Moriyama ◽  
Tadashi Ogawa ◽  
Shinichi Kawamoto

PROTEOMICS ◽  
2009 ◽  
Vol 9 (7) ◽  
pp. 1827-1840 ◽  
Author(s):  
Woon-Won Jung ◽  
Sohee Phark ◽  
Sangnam Oh ◽  
Jin-Young Khim ◽  
Juneyoung Lee ◽  
...  

2014 ◽  
Vol 51 (2) ◽  
pp. 283-290
Author(s):  
Stanisław Weidner ◽  
Kazimierz Zalewski

It was found, by comparing the densitometric profiles of ribosomal proteins of wheat embryos in milk and full grain ripeness, that in the process of development and ripening of caryopses the percentual proportion of low molecular weight proteins increases at the cost of those of high molecular weight. This concerns both acidic and basic proteins. In electrophoretic separation of ribosomal proteins from embryos of fully ripe seeds by the method of two-dimensional electrophoresis the appearance of three new low molecular weight proteins - an acidic one and two basic ones - was observed. These proteins were not found in the embryos of caryopses of milk ripeness. These results indicate that with development and ripening of wheat caryopses new low molecular weight ribosomal proteins are built into the ribosomes in the embryo. These changes are both quantitative and qualitative.


1998 ◽  
Vol 28 (1) ◽  
pp. 25-32 ◽  
Author(s):  
I.M. Verbruggen ◽  
W.S. Veraverbeke ◽  
A. Vandamme ◽  
J.A. Delcour

1986 ◽  
Vol 28 (1) ◽  
pp. 76-83 ◽  
Author(s):  
P. R. Shewry ◽  
S. Parmar ◽  
N. Fulrath ◽  
D. D. Kasarda ◽  
T. E. Miller

The chromosomal locations of the structural genes for secalin storage proteins in Secale cereale and S. montanum were determined by electrophoresis of grain proteins from wheat–rye addition and substitution lines. The use of several different extraction procedures and high-resolution electrophoretic systems (one and two dimensional) enabled us to demonstrate that the genes for all the high molecular weight secalins are present on chromosome IRL, and for all the ω-secalins and at least some of the γ-secalins with a relative molecular mass (Mr) of 40 000 on chromosome IRS of both species. In contrast, the genes for the γ-secalins (Mr = 75 000) are located on 2RcS in S. cereale but 6Rm in S. montanum. These observations are discussed in relation to evolution of prolamins and their genes in Secale and related members of the Triticeae.Key words: Secale, rye, seed proteins, structural genes, two-dimensional electrophoresis.


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