scholarly journals The main seed storage proteins among high-protein soybean genotypes

Genetika ◽  
2008 ◽  
Vol 40 (1) ◽  
pp. 9-16 ◽  
Author(s):  
Ksenija Taski-Ajdukovic ◽  
Vuk Djordjevic ◽  
Milos Vidic ◽  
Milka Vujakovic ◽  
Mirjana Milosevic ◽  
...  

It is known that the main components of the seed storage proteins contribute to the quality of soybean [Glycine max (L.) Merr.] food products. The objective of this study was to investigate content of the two of them [glycinin (11S) and ?-conglycinin (7S) fractions] and their respective subunits on the new high-protein soybean genotypes from the Institute for Field and Vegetable Crops, Novi Sad, Serbia. Subunits were resolved by SDS-PAGE and gels were analyzed by scanning densitometry. Out of 20 analyzed genotypes, the ?' and ? subunits of ?- conglycinin were significantly higher in all of the genotypes except KO531 and KO5431. The ? subunit of ?-conglycinin was significantly higher in genotypes KO535 KO5437, KO534, KO537, KO539, KO5439, KO532, KO5435, KO538, KO5438 and KO533. The acetic polypeptides of glycinin were significantly higher in genotypes KO5439, KO5437, KO5436, KO5438, KO5432, KO5435, KO5433 and KO5434. The basic polypeptides of glycinin were not significantly higher only in genotypes KO539, KO536, KO538, KO535 and KO533. In conclusion, it appears that among the new high-protein genotypes there are genotypes with different amount of subunits that should be bread in the future for a desired level of the protein components. .

2010 ◽  
Vol 45 (7) ◽  
pp. 721-729 ◽  
Author(s):  
Ksenija Taski-Ajdukovic ◽  
Vuk Djordjevic ◽  
Milos Vidic ◽  
Milka Vujakovic

The objective of this work was to quantify the accumulation of the major seed storage protein subunits, β-conglycinin and glycinin, and how they influence yield and protein and oil contents in high-protein soybean genotypes. The relative accumulation of subunits was calculated by scanning SDS-PAGE gels using densitometry. The protein content of the tested genotypes was higher than control cultivar in the same maturity group. Several genotypes with improved protein content and with unchanged yield or oil content were developed as a result of new breeding initiatives. This research confirmed that high-protein cultivars accumulate higher amounts of glycinin and β-conglycinin. Genotypes KO5427, KO5428, and KO5429, which accumulated lower quantities of all subunits of glycinin and β-conglycinin, were the only exceptions. Attention should be given to genotypes KO5314 and KO5317, which accumulated significantly higher amounts of both subunits of glycinin, and to genotypes KO5425, KO5319, KO539 and KO536, which accumulated significantly higher amounts of β-conglycinin subunits. These findings suggest that some of the tested genotypes could be beneficial in different breeding programs aimed at the production of agronomically viable plants, yielding high-protein seed with specific composition of storage proteins for specific food applications.


2007 ◽  
Vol 100 (4) ◽  
pp. 1324-1327 ◽  
Author(s):  
J.G. Manjaya ◽  
K.N. Suseelan ◽  
T. Gopalakrishna ◽  
S.E. Pawar ◽  
V.A. Bapat

2010 ◽  
Vol 16 (1) ◽  
pp. 53-58 ◽  
Author(s):  
Prachi Gupta ◽  
Rohtas Singh ◽  
S. Malhotra ◽  
K. S. Boora ◽  
H. R. Singal

2014 ◽  
Vol 59 (3) ◽  
pp. 359-363 ◽  
Author(s):  
Seong-Woo Cho ◽  
Soo-Jeong Kwon ◽  
Swapan Kumar Roy ◽  
Hong-Sig Kim ◽  
Chul-Won Lee ◽  
...  

2013 ◽  
Vol 781-784 ◽  
pp. 1717-1722
Author(s):  
Yue Hui Liu ◽  
Jun Wang ◽  
Xin Chao Yang ◽  
Na Xin Sun ◽  
Li Hua Xu

A convenient way of producing effective antibody against maize seed storage proteins is present.The protein patterns of maize hybrid seed Ludan50 have two special protein bands with Polyacrylamide gel electrophoresis (PAGE) which was corresponding to its parent inbred lines Luyuan92 and Qi319. We purified the two proteins respectively by acid-PAGE and then immunized rabbit and laying hens, obtained the antiserums and yolk antibodies. Both antiserums and yolk antibodies have good specificity against the antigens, except that the yolk antibody has a higher titer. We also measured its specificity against different protein components extracted with pure water, 2.5% NaCl (w/v) , 70%(v/v) alcohol , 10mM HCl and 50mM KOH. The results appears that the water-soluble proteins tended to be more specific than othors to the antibodies, so the two inbred lines can be identified from each other by ELISA with the antibody we have been produced.


Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.


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