Soybean / -conglycinin

Fig. 3. Sodium dodecyl sulfate—polyacrylamide gel electrophoretic pattern for molecular weight standards (lane 1) water-extractable proteins of defatted soybean meal (lane 2) purified IIS (glycinin) (lane 3) and purified 7S (P-conglycinin) (lane 4) where the numbers represent mol wt x 10. The gel was mn in the presence of 2-mercaptoethanol, resulting in the cleavage of the disulfide bond linking the acidic (A bands) and basic (B bands) polypeptides of the...

Chen, H. M., Muramoto, K., and Yamauchi, F. (1995). Structural analysis of antioxidative peptides from soybean p-conglycinin. ]. Agric. Food Chem. 43, 574—578. 

Samoto, M., Fukuda, Y., Takahashi, K., Tabuchi, K., Hiemori, M., Tsuji, H., Ogawa, T., Kawamura, Y. 1997. Substantially complete removal of three major allergenic soybean proteins (Gly m Bd 30 K, Gly m Bd 28 K, and the alpha subunit of conglycinin) from soy protein by using a mutant soybean, Tohoku 124. Biosci Biotechnol Biochem 61 2148-2150. 

Shutov, A.D., Kakhovskaya, I.A., Bastrygina, A.S., Bulmaga, V.P, Horstmann, C., Muntz, K. 1996. Limited proteolysis of P-conglycinin and glycinin, the 7s and 11s storage globulins from soybean (Glycine max (L.) Merr.) Structural and evolutionary implications. Eur J Biochem 241 221-228. 

Takahashi, K., Banba, H., Kikuchi, A., Ito, M., Nakamura, S. 1994. An induced mutant line lacking the a-subunit of P-conglycinin in soybean (Glycine max (L) Merril). Breeding Sci 44 65-66. 

Soybean proteins are packaged in discrete spherical subcellular structures called protein bodies in the palisade-like cells of the soybean cotyledons (Bair Snyder, 1980). The soybean storage protein structures for glycinin and P-conglycinin are apparently highly conserved to maximize protein packaging in the protein bodies (Shewry et ah. 

Davies, C.S. J.B. Coates N.C. Nielsen. Inheritances and biochemical analysis of four electrophoretic varieants of 3-conglycinin from soybean. Jheor. AppL Genetics 1985, 71, 351—308. 

Galyer, K.R. G.E. Sykes. Beta-conglycinins in developing soybean seeds. Plant Physiol. 1981, 67(5), 958-961. 

Krishnan, H.B. S.S. Natarajan A.A. Mahmoud R. Nelson. Identification of glycinin and P-conglycinin subunits that contribute to the increased protein content of high-protein soybean lines./. Agric. Food Chem. 2007, 55, 1839-1845. 

Maruyama, N. T. Katsybe Y. Wada M.H. Oh A.P. Barba de la Rosa E. Okuda S. Nakagawa S. Utsumi. The roles of the N-linked glycans and extension regions of soybean P-conglycinin in folding, assembly and structural features. Eur. J. Biochem. 1998, 258, 854-862. 

Maruyama, N. M.R.M. Salleh K.I. Takahashi K. Yagasaki H. Goto N. Hontani S. Nakagawa S. Utsumi. The effect of the N-linked glycoans on structural features and physicochemical functions of soybean P-conglycinin homotrimers./. Am.. Oil Chem. Soc. 2002a, 79, 134-144. 

Maruyama, Y N. Maruyama B. Mikami S. Utsumi. Structure of the core region of the soybean P-conglycinin a subunit. Acta Crystallogr. 2004, D60, 289-297. 

Maruyama, N. M. Adachi K. Takahashi K. Yagasaki M. Kohno Y. Takenaka E. Okuda S. Nakagawa B. Mikami S. Utsumi. Crystal structures of recombinant and native soybean P-conglycinin P homotrimers. Eur. J. Biochem. 2001, 268, 3595-3604. 

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