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Title: PROTEOMIC ANALYSIS OF BETA-GONGLYCININ AND GLYCININ IN DIFFERENT SOYBEAN GENOTYPES

Author
item Natarajan, Savithiry - Savi
item Cregan, Perry
item XU, CHENPING - UNIVERSITY OF MARYLAND
item Caperna, Thomas
item Garrett, Wesley
item SULLIVAN, JOSEPH - UNIVERSITY OF MARYLAND

Submitted to: Mid Atlantic Plant Molecular Biology Society Conference
Publication Type: Abstract Only
Publication Acceptance Date: 10/1/2005
Publication Date: 10/1/2005
Citation: Natarajan, S.S., Cregan, P.B., Xu, C., Caperna, T.J., Garrett, W.M., Sullivan, J. 2005. Proteomic analysis of beta-gonglycinin and glycinin in different soybean genotypes [abstract]. Mid Atlantic Plant Molecular Biology Society Conference. Paper No. 7.

Interpretive Summary:

Technical Abstract: Beta-conglycinin and glycinin are two major storage proteins that together comprise 70 to 80 % of the total seed protein. In this study, we have investigated variation of beta-conglycinin and glycinin (acidic and basic) in cultivated and wild soybean seeds using 2-D gel electrophoresis and mass spectrometry based proteomic techniques. We have chosen four cultivated Glycine max accessions (PI 423954, PI 89138, PI 594777 and PI 59845) and four wild Glycine soja accessions (PI 407027, PI 407282, PI 366120, and PI 393551) and compared seed protein variation. Our results showed all wild, G. soja genotypes have a total of thirteen beta-conglycinin subunits (alpha subunit of beta-conglycinin, alpha subunit of beta-conglycinin and beta subunit of beta-conglycinin) when compared to eleven in G. max genotypes. The cultivated soybeans had 14-20 acidic and basic subunits of glycinin whereas the wild genotype soybeans contained 19-22 acidic and basic subunits. Our data indicated that there were major variations of protein profiles between cultivated and wild soybean seeds rather than among accessions of the same species.