Structural and Functional Analysis of Various Globulin Proteins from Soy Seed

REFERENCES

• Adachi, M., Kanamori, J., Masuda, T., Yagasaki, K., Kitamura, K., Mikami, B. and Utsumi, S. (2003). Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer. Proc. Nat. Acad. Sci. USA 100:7395–7400.
   PubMed Web of Science ®Google Scholar
• Adachi, M., Takenaka, Y., Gidamis, A. B., Mikami, B. and Utsumi, S. (2001). Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 305:291–305.
   PubMed Web of Science ®Google Scholar
• Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D. J. (1997). Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:(17):3389–3402.
   PubMed Web of Science ®Google Scholar
• Aoyama, T., Kohno, M., Saito, T., Fukui, K., Takamatsu, K., Yamamoto, T., Hashimoto, Y., Hirotsuka, M. and Kito, M. (2001). Reduction by phytate-reduced soybean b-conglycinin of plasma triglycerides level of young and adult rats. Biosci. Biotechnol. Biochem. 65:(5):1071–1075.
   PubMed Web of Science ®Google Scholar
• Asakura, T., Tamura, T., Terauchi, K., Narikawa, T., Yagasaki, K., Ishimaru, Y. and Abe, K. (2012a). Global gene expression profiles in developing soybean seeds. Plant Physiol. Biochem. 52:147–153.
   PubMed Web of Science ®Google Scholar
• Asakura, T., Tamura, T., Terauchi, K., Narikawa, T., Yagasaki, K., Ishimaru, Y. and Abe, K. (2012b). Global gene expression profiles in developing soybean seeds. Plant Physiol. Bio. 52:147–153.
   PubMed Web of Science ®Google Scholar
• Badley, R. A., Atkinson, D., Hauser, H., Oldani, D., Green, J. P. and Stubbs, J. M. (1975). The structure, physical and chemical properties of the soybean protein glycinin. Biochim. Biophys. Acta 412(2):214–228.
   PubMed Web of Science ®Google Scholar
• Beachy, R. N., Chen, Z. L., Horsch, R. B., Rogers, S. G., Hoffman, N. J. and Fraley, R. T. (1985). Accumulation and assembly of soybean β-conglycinin in seeds of transformed petunia plants. EMBO J. 4(12):3047–3053.
   PubMed Web of Science ®Google Scholar
• Beachy, R. N., Jarvis, N. P. and Barton, K. A. (1981). Biosynthesis of subunits of the soybean 7S storage protein. J. Mol. Appl. Genet. 1:19–27.
   PubMedGoogle Scholar
• Beilinson, V., Chen, Z., Shoemaker, C., Fischer, L., Goldberg, B. and Nielsen, C. (2002). Genomic organization of glycinin genes in soybean. TAG Theor. Appl. Genet. Theoretische und Angew. Genetik 104:1132–1140.
   PubMed Web of Science ®Google Scholar
• Catsimpoolas, N. (1968). Micro isoelectric focusing in polyacrylamide gel columns. Anal. Biochem. 26:480–482.
   PubMed Web of Science ®Google Scholar
• Catsimpoolas, N. (1969). A note on the proposal of an immunochemical system of reference and nomenclature for the major soybean globulins. Cereal Chem. 46:369–372.
   Web of Science ®Google Scholar
• Catsimpoolas, N. and Ekenstam, C. (1969). Isolation of alpha, beta, and gamma conglycinins. Arch. Biochem. Biophys. 129:490–497.
   PubMed Web of Science ®Google Scholar
• Chen, L., Pan, N. S. and Beachy, R. N. (1988). A DNA sequence element that confers seed-specific enhancement of a constitutive promoter. EMB0 J. 7:6.
   Google Scholar
• Chen, L., Schuler, M. A. and Beachy, R. N. (1986). Functional analysis of regulatory elements in a plant embryo-specific gene. Proc. Natl. Acad. Sci. U S A 83:5.
   Google Scholar
• Chen, A. and Shoemaker, R. (1998). Four genes affecting seed traits in soybeans map to linkage group F. J. Hered. 89:211–215.
   Web of Science ®Google Scholar
• Cho, S. J., Iuillerat, M. A. and, Lee, C. H. (2008). Identification of LDL-receptor transcription stimulating peptides from soybean hydrolysate in human hepatocytes. J. Agric. Food Chem. 56:4372–7376.
   PubMed Web of Science ®Google Scholar
• Cho, T. J. and Nielsen, N. C. (1989). The glycinin Gy3 gene from soybean. Nucleic Acids Res. 17:4388.
   PubMed Web of Science ®Google Scholar
• Chrispeels, M. J. (1991). Sorting of proteins in the secretory system. Annu. Rev. Plant Phys. 42:21–53.
   Web of Science ®Google Scholar
• Chrispeels, M., Higgins, T. and Spencer, D. (1982). Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J. Cell Biol. 93:306–313.
   PubMed Web of Science ®Google Scholar
• Consonni, A., Lovati, M. R., Parolari, A., Manzoni, C., Morazzoni, P., Magni, C. and Duranti, M. (2011). Heterologous expression and purification of the soybean 7S globulin alpha’ subunit extension region: In vitro evidence of its involvement in cell cholesterol homeostasis. Protein Expr. Purif. 80:125–129.
   PubMed Web of Science ®Google Scholar
• Davies, C. S., Cho, T.J., and Nielsen, N. C. (1987). Tests for linkage of seed protein genes Lxl, Lx3, and Cgyl to markers on known linkage groups. Soybean Genet. Newsl. 14:5.
   Google Scholar
• Davies, C. S., Coates, C. J. and Nielsen, N. C. (1985). Inheritance and biochemical analysis of four electrophoretic variants of β-conglycinin from soybean. TAG Theor. Appl. Genet. Theoretische und Angew. Genetik 71:351–358.
   PubMed Web of Science ®Google Scholar
• Derbyshire, E., Wright, D. J. and Boulter, D. (1976). Legumin and vicilin, storage proteins of legume seeds. Phytochem. 15:3–24.
   Web of Science ®Google Scholar
• Dickinson, C. D., Evans, R. P. and Nielsen, N. C. (1988). RYrepeats are conserved in the 5'-flanking regions of legume seed-protein genes. Nucl. Acids Res. 16.
   PubMed Web of Science ®Google Scholar
• Dickinson, C. D., Hussein, H. E. and Nielsen, N. C. (1989). Role of posttranslational cleavage in glycinin assembly. Plant cell 1(4):459–469.
   PubMed Web of Science ®Google Scholar
• Diers, B. W., Beilinson, V., Nielsen, N. C. and Shoemaker, R. C. (1994). Genetic mapping of the Gy4 and Gy5 glycinin genes in soybean and the analysis of a variant of Gy4. Theor. Appl. Genet. 89:297–304.
   PubMed Web of Science ®Google Scholar
• Dorel, C., Voelker, T. A., Herman, E. M. and Chrispeels, M. J. (1989). Transport of proteins to the plant vacuole is not by bulk flow through the secretory system, and requires positive sorting information. J. Cell Biol. 108:327–337.
   PubMed Web of Science ®Google Scholar
• Doyle, J. J., Schuler, M. A., Godette, W. D., Zenger, V., Beachy, R. N. and Slightom, J. L. (1986). The glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris: Structural homologies of genes and proteins. J. Biol. Chem. 261:11.
   Google Scholar
• Dunwell, J. M., Khuri, S. and Gane, P. J. (2000). Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily. Microbiol. Mol. Biol. Rev. 64:153–179.
   PubMed Web of Science ®Google Scholar
• Ereken-Tumer, N., Richter, J. D. and Nielsen, N. C. (1982). Structural characterization of the glycinin precursor. J. Biol. Chem. 257:4016–4018.
   PubMed Web of Science ®Google Scholar
• Fassini, P. G., Noda, R. W., Ferreira, E. S., Silva, M. A., Neves, V. A. and Demonte, A. (2011). Soybean glycinin improves HDL-C and suppresses the effects of rosuvastatin on hypercholesterolemic rats. Lipids Health Dis. 10:165.
   PubMed Web of Science ®Google Scholar
• Ferreira, E., Silva, M., Demonte, A. and Neves, V. (2012). Beta-conglycinin combined with fenofibrate or rosuvastatin have exerted distinct hypocholesterolemic effects in rats. Lipids Health Dis. 11:11.
   PubMed Web of Science ®Google Scholar
• Fischer, R. L. and Goldberg, R. B. (1982). Structure and flanking regions of soybean seed protein genes. Cell 29:651–660.
   PubMed Web of Science ®Google Scholar
• Fitzgerald, M., and Shenk, T. (1981). The sequence 5'-AAUAAA-3' forms part of the recognition site for polyadenylation of late SV40 mRNAs. Cell 24:10.
   PubMed Web of Science ®Google Scholar
• Fumio, Y., Masaaki, S., Wataru, S., Yoshiro, K. and Kazuo, S. (1981). Isolation and identification of a new type of β-conglycinin in soybean globulins. Agr. Biol. Chem. 45:2863–2868. http://ci.nii.ac.jp/naid/130000028688/en/
   Google Scholar
• Garner, M. E., Hymowitz, T., Xu, S. J. and Hartman, G. L. (2001). Physical map location of the Rps1-k allele in soybean. Crop Sci. 41(5):1435–1438.
   Web of Science ®Google Scholar
• Geldberg, R. B. (1986). Regulation of plant gene expression. Philos. Trans. R. Soc. Lond B Biol. Sci. 314:11.
   Google Scholar
• Goldberg, R. B., Hoscheck, G., Ditta, G. S. and Breidenbach, R. W. (1981a). Developmental regulation of clone superabundant embryo mRNAs in soybean. Dev. Biol. 83:14.
   Google Scholar
• Goldberg, R. B. and Sims, T. L. (1989). The glycinin Gy1 gene from soybean. Nucleic Acids Res. 17(11):4386.
   PubMed Web of Science ®Google Scholar
• Harada, J. J., Barker, S. J. and Goldberg, R. B. (1989). Soybean b-conglycinin genes are clustered in several DNA regions and are regulated by transcriptional and posttranscriptional processes. Plant Cell 1:415–425.
   PubMed Web of Science ®Google Scholar
• Hara-Nishimura, I. and Nishimura, M. (1987). Proglobulin processing enzymes in vacuoles isolated from developing pumpkin cotyledons. Plant Phys. 85:440–455.
   PubMed Web of Science ®Google Scholar
• He, F., Huang, F., Wilson, K. A. and Tan-Wilson, A. (2007). Protein storage vacuole acidification as a control of storage protein mobilization in soybeans. J. Exp. Bot. 58(10):2391–2407.
   PubMed Web of Science ®Google Scholar
• Hill, J. E. and Breidenbach, R. W. (1974). Proteins of soybean seeds: I. isolation and characterization of the major components. Plant Phys. 53:742–746.
   PubMed Web of Science ®Google Scholar
• Hirano, H., Kagawa, H., Kamata, Y. and Yamauchi, F. (1986). Structural homology among the major 7s globulin subunits of soybean seed storage proteins. Phytochem. 26:41–45.
   Web of Science ®Google Scholar
• Hirano, H., Kagawa, H. and Okubo, K. (1992). Characterization of proteins released from legume seeds in hot water. Phytochem. 31:731–735..
   PubMed Web of Science ®Google Scholar
• Hirano, H. and Watanabe, T. (1990). Microsequencing of proteins electrotransferred onto immobilizing matrices from polyacrylamide gel electrophoresis: Application to an insoluble protein. Electroph. 11:573–580.
   PubMed Web of Science ®Google Scholar
• Hofmann, K., Bucher, P., Falquet, L. and Bairoch, A. (1999). The Prosite database, its status in 1999. Nucleic Acids Res. 27:215–219.
   PubMed Web of Science ®Google Scholar
• Holm, L. and Rosenstrom, P. (2010). Dali server: conservation mapping in 3D. Nucleic Acids Res. 38(Suppl. 2):W545–W549.
   Google Scholar
• Hu, B. and Esen, A. (1981). Heterogeneity of soybean seed proteins: One-dimensional electrophoretic profiles of six different solubility fractions. J. Agr. Food Chem. 29:497–501.
   PubMed Web of Science ®Google Scholar
• Hu, B. and Esen, A. (1982). Heterogeneity of soybean proteins: Two-dimensional electrophoretic maps of three solubility fractions. J. Agr. Food Chem. 30:21–25.
   Web of Science ®Google Scholar
• Kagawa, H., and Hirano, H. (1989). Sequence of a cDNA encoding soybean basic 7S globulin. Nucleic Acids Res. 17:8868.
   PubMed Web of Science ®Google Scholar
• Kagawa, H., Yamauchi, F. and Hirano, H. (1987). Soybean basic 7S globulin represents a protein widely distributed in legume species. FEBS Lett. 226:145–149.
   Web of Science ®Google Scholar
• Kambara, H., H. M., Takamatsu, K. and Kito, M. (2002). Triglyceride-lowering effect of soybean b-conglycinin in humans. Ther. Res. 23:85–89.
   Google Scholar
• Kaviani, B. and Kharabian, A. (2008). Improvement of the nutritional value of soybean [Glycine max (L.) Merr.] seed with alteration in protein subunit of glycinin (11S globulin) and beta-conglycinin (7S globulin). Turk. J. Biol. 32:91–97.7.
   Web of Science ®Google Scholar
• Kim, H. T., Choi, U. K., Ryu, H. S., Lee, S. J. and Kwon, O. S. (2011b). Mobilization of storage proteins in soybean seed (Glycine max L.) during germination and seedling growth. Biochim. Biophys. Acta 1814:1178–1187.
   PubMed Web of Science ®Google Scholar
• Kinsella, J. (1979). Functional properties of soy proteins. J. Am. Oil Chem. Soc. 56:242–258.
   Web of Science ®Google Scholar
• Komatsu, S. and Hirano, H. (1991). Plant basic 7S globulin-like proteins have insulin and insulin-like growth factor binding activity. FEBS Lett. 294:210–212.
   PubMed Web of Science ®Google Scholar
• Komatsu, S., Koshio, O., and Hirano, H. (1994). Protein kinase activity and insulin-binding activity in plant basic 7S globulin. Biosci. Biotech. Bioch. 58:1705–1706. http://ci.nii.ac.jp/naid/110002677179/en/
   PubMed Web of Science ®Google Scholar
• Koshiyama, I. (1965). Purification of the 7S component of soybean proteins. Agric. Biol. Chem. 29:3.
   Google Scholar
• Koshiyama, I. (1968a). Chemical and physical properties of a 7S protein in soybean globulins. Cereal. Chem. 10.
   Google Scholar
• Koshiyama, I. (1968b). Factors influencing conformation changes in a 7S protein of soybean globulins by ultracentrifugal investigations. Agric. Bioi. Chern. (Tokyo) 9.
   Google Scholar
• Koshiyama, I. and Fukushima, D. (1976a). Identification of the 7S globulin with β-conglycinin in soybean seeds. Phytochem. 15:157–159.
   Web of Science ®Google Scholar
• Koshiyama, I. and Fukushima, D. (1976b). Purification and some properties of γ-conglycinin in soybean seeds. Phytochem. 15:161–164.
   Web of Science ®Google Scholar
• Krishnan, H. B. and Nelson, R. L. (2011). Proteomic analysis of high protein soybean (Glycine max) accessions demonstrates the contribution of novel glycinin subunits. J. Agr. Food Chem. 59:2432–2439.
   PubMed Web of Science ®Google Scholar
• Lee, J., Zou. J. J., Xu, S., Kollipara, K. P., Cregan, P. B., Singh, R. J. and Hymowitz, T. (2000). Development of the universal soybean map. 8th Biennial Conf Cellular and Mol Biol of the Soybean.
   Google Scholar
• Lelievre, J. M., Dickinson, C., Dickinson, L. A. and Nielsen, N. C. (1992). Synthesis and assembly of soybean β-conglycinin in vitro. Plant Mol. Biol. 18:259–274.
   PubMed Web of Science ®Google Scholar
• Li, C. and Zhang, Y. M. (2011). Molecular evolution of glycinin and beta-conglycinin gene families in soybean (Glycine max L. Merr.). Heredity 106:633–641.
   PubMed Web of Science ®Google Scholar
• Liu, X., Zhang, Z., Barnaby, N., Wilson, K. A. and Tan-Wilson, A. (2001). Soybean subtilisin-like protease involved in initiating storage protein degradation. Seed Sci. Res. 11:14.
   Web of Science ®Google Scholar
• Lovati, M. R., West, C. M., Canavesi, A., Sirtori, M., Vaccarini, V., Marchi, M., Gaddi, G. and Sirtori, C. R. (1987). Soybean protein diet increases low-density lipoprotein receptor activity in mononuclear cells from hypercholesterolemic patients. J. Clin. Invest. 80:125–130.
   Web of Science ®Google Scholar
• Lovati, M. R., West, C. M., Corsini, A., Granata, A., Frattini, R., Fumagalli, R. and Sirtori, C. R. (1992). Low-density receptor activity is modulated by soybean globulins in cell culture. J. Nutr. 122:1971–1978.
   PubMed Web of Science ®Google Scholar
• Lo Conte, L., Ailey, B., Hubbard, T. J., Brenner, S. E., Murzin, A. G., and Chothia, C. (2000). SCOP: A structural classification of proteins database. Nucleic Acids Res. 28(1):257–259.
   PubMed Web of Science ®Google Scholar
• Lutcke, H. A., Chow, K. C., Mickel, F. S., Moss, K. A., Kern, H. F. and Scheele, G. A. (1987). Selection of AUG differs in plants and animals. EMBO J. 6:6.
   Google Scholar
• Manzoni, C., Duranti, M., Eberini, I., Scharnag, H., Marz, W., Castiglioni, S. and Lovati, M. R. (2003). Subcellular localization of soybean 7S globulin in HepG2 cells and LDL receptor up-regulation by its alpha’ constituent subunit. J. Nutr. 133:2149–2155.
   PubMed Web of Science ®Google Scholar
• Maruyama, N., Katsube, T., Wada, Y., Oh, M. H., Barba De La Rosa, A. P., Okuda, E., Nakagawa, S. and Utsumi, S. (1998). The roles of the N-linked glycans and extension regions of soybean beta-conglycinin in folding, assembly and structural features. Eur. J. Biochem./FEBS 258:854–862.
   PubMedGoogle Scholar
• Meinke, D. W., Chen, J. and Beachy, R. N. (1981). Expression of storage-protein genes during soybean seed development. Planta 153:130–139.
   PubMed Web of Science ®Google Scholar
• Nam, Y. W., Jung, R. and Nielsen, N. C. (1997). Adenosine 5’-triphosphate is required for the assembly of 11S seed proglobulins in vitro. Plant Phys. 115(4):1629–1639.
   PubMed Web of Science ®Google Scholar
• Nicholas, C. (1969). Isolation of glycinin subunits by isoelectric focusing in urea-mercaptoethanol. FEBS Lett. 4:259–261.
   PubMed Web of Science ®Google Scholar
• Nielsen, N. C. (1984). The chemistry of legume storage proteins. Philos. Trans. Roy. Soc. London B, Biol. Sci. 304:287–296.
   Web of Science ®Google Scholar
• Nielsen, N. (1985). The structure and complexity of the 11S polypeptides in soybeans. J. Am. Oil Chem. Soc. 62:1680–1686.
   Web of Science ®Google Scholar
• Nielsen, N. C., Dickinson, C. D., Cho, T. J., Thanh, V. H., Scallon, B. J., Fischer, R. L., Sims, T. L., Drews, G. N. and Goldberg, R. B. (1989). Characterization of the glycinin gene family in soybean. Plant Cell 1:313–328.
   PubMed Web of Science ®Google Scholar
• Nishizawa, N. K., Mori, S., Watanabe, Y. and Hirano, H. (1994). Ultrastructural localization of the basic 7S globulin in soybean (Glycine max) cotyledons. Plant Cell Phys. 35:1079–1085.
   Web of Science ®Google Scholar
• Qi, X., Chen, R., Wilson, K. A. and Tan-Wilson, A. L. (1994). Characterization of a soybean b-conglycinin-degrading protease cleavage site. Plant Phys. 104:127–133.
   PubMed Web of Science ®Google Scholar
• Qi, X., Wilson, K. A. and Tan-Wilson, A. L. (1992). Characterization of the major protease involved in the soybean beta-conglycinin storage protein mobilization. Plant Phys. 99(2):725–733.
   PubMed Web of Science ®Google Scholar
• Sato, K., Yamagishi, T., Kamata, Y. and Yamauchi, F. (1987). Subunit structure and immunological properties of a basic 7s globulin from soybean seeds. Phytochem. 26:903–908.
   Web of Science ®Google Scholar
• Schuler, M. A., Ladin, B. F., Pollaco, J. C., Freyer, G. and Beachy, R. N. (1982). Structural sequences are conserved in the genes coding for the α, α′ and β-subunits of the soybean 7S seed storage protein. Nucleic Acids Res. 10:8245–8261.
   PubMed Web of Science ®Google Scholar
• Sengupta, C., Deluca, V., Bailey, D. S. and Verma, D. P. S. (1981a). Post-translational processing of 7S and 11S components of soybean storage proteins. Plant Mol. Biol. 1:19–34.
   PubMedGoogle Scholar
• Sengupta, C., Deluca, V., Bailey, D. S. and Verma, D. P. S. (1981b). Posttranscriptional processing of 7s and 11 S components of soybean storage proteins. Plant Mol. Biol. 1:16.
   Google Scholar
• Seo, S., Tan-Wilson, A. and Wilson, K. A. (2001). Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins. Biochim. Biophys. Acta 1545:192–206.
   PubMed Web of Science ®Google Scholar
• Sirtori, C. R. and Lovati, M. R. (2001). Soy protein and cardiovascular disease. Curr. Atheroscler. Rep. 3(1):47–53.
   PubMedGoogle Scholar
• Staswick, P. E., Hermodson, M. A. and Nielsen, N. C. (1981). Identification of the acidic and basic subunit complexes of glycinin. J. Biol. Chem. 256:8752–8755.
   PubMed Web of Science ®Google Scholar
• Staswick, P. E., Hermodson, M. A., and Nielsen, N. C. (1984). Identification of the cystines which link the acidic and basic components of the glycinin subunits. J. Biol. Chem. 259:13431–13435.
   PubMed Web of Science ®Google Scholar
• Tachibana, N., Iwaoka, Y., Hirotsuka, M., Horio, F. and Kohno, M. (2010). β-Conglycinin lowers very-low-density lipoprotein-triglyceride levels by increasing adiponectin and insulin sensitivity in rats. Biosci. Biotech. Bioch. 74:1250–1255.
   PubMed Web of Science ®Google Scholar
• Thant, V. H., Turner, N. E. and Nielsen, N. C. (1989). The glycinin Gy2 gene from soybean. Nucleic Acids Res. 17:4387.
   PubMed Web of Science ®Google Scholar
• Tombs, M. P. (1967). Protein bodies of the soybean. Plant Phys. 42:797–813.
   PubMed Web of Science ®Google Scholar
• Tsukada, Y., Kitamura, K., Harada, K., and Kaizumu, N. (1986). Genetic analysis of subunits of two major storage protein (β-conglycinin and glycinin) in soybean seeds. JPN J. Breed. 36:390–400.
   Web of Science ®Google Scholar
• Tumer, N. E., Thanh, V. H. and Nielsen, N. C. (1981). Purification and characterization of mRNA from soybean seeds. Identification of glycinin and beta-conglycinin precursors. J. Biol. Chem. 256:8756–8760.
   PubMed Web of Science ®Google Scholar
• Utsumi, S., Matsumura, Y. and Mori, T. (1997). Structure-function relationships of soy proteins, in Damodaran, S. and Paraf, A., Food Proteins and Their Applications. New York, NY: Marcel Dekker, 1997, pp 257–291.
   Google Scholar
• Vu Huu, T. and Kazuo, S. (1977). Beta-conglycinin from soybean proteins. Isolation and immunological and physicochemical properties of the monomeric forms. Biochim. Biophys. Acta (BBA) Protein Struct. 490:370–384.
   PubMed Web of Science ®Google Scholar
• Vu Huu, T. and Shibasaki, K. (1978). Major proteins of soybean seeds. Subunit structure of .beta.-conglycinin. J. Agr. Food Chem. 26:692–695.
   Web of Science ®Google Scholar
• Wadahama, H., Iwasaki, K., Matsusaki, M., Nishizawa, K., Ishimoto, M., Arisaka, F., Takagi, K. and Urade, R. (2012). Accumulation of β-conglycinin in soybean cotyledon through the formation of disulfide bonds between α′- and α-subunits. Plant Phys. 158:1395–1405.
   PubMed Web of Science ®Google Scholar
• Walling, L., Drews, G. N. and Goldberg, R. B. (1986). Transcriptional and posttranscriptional regulation of soybean seed protein mRNA levels. Proc. Natl. Acad. Sci. U S A 83:5.
   Web of Science ®Google Scholar
• Watanabe, Y. and Hirano, H. (1994). Nucleotide sequence of the basic 7S globulin gene from soybean. Plant Phys. 105:1019–1020.
   PubMed Web of Science ®Google Scholar
• Wilson, K. A., Rightmire, B. R., Chen, J. C. and Tan-Wilson, A. L. (1986). Differential proteolysis of glycinin and beta-conglycinin polypeptides during soybean germination and seedling growth. Plant Phys. 82:71–76.
   PubMed Web of Science ®Google Scholar
• Wolf, W. T. T. (1969). Heat denaturation of soybean 11S protein. Cereal Chem. 46:14.
   Google Scholar
• Wolf, W. J. and Nelsen, T. C. (1996). Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin. J. Agr. Food Chem. 44:785–791.
   Web of Science ®Google Scholar
• Wolf, W. J., Rackis, J. J., Smith, A. K., Sasame, H. A. and Babcock, G. E. (1958). Behavior of the 11S protein of soybeans in acid solutions. I. Effects of pH, ionic strength and time on ultracentrifugal and optical rotatory properties. J. Am. Chem. Soc. 80:5730–5735.
   Web of Science ®Google Scholar
• Yagasaki, , Kaizuma, N., and Kitamura, K. (1996). Inheritance of glycinin subunits and characterization of glycinin molecules lacking the subunits in soybean (Glycine max L. Merr.). Breed. Sci. 46:251–255.
   Google Scholar
• Yamauchi, F., Sato, K. and Yamagishi, T. (1984). Isolation and partial characterization of a salt-extractable globulin from soybean seeds. Agric. Biol. Chem. 48:645.
   Web of Science ®Google Scholar
• Yamazaki, T., Kishimoto, K., Miura, S. and Ezaki, O. (2012). Dietary β-conglycinin prevents fatty liver induced by a high-fat diet by a decrease in peroxisome proliferator-activated receptor γ2 protein. J. Nutr. Biochem. 23:123–132.
   PubMed Web of Science ®Google Scholar
• Yoshino, M., Kanazawa, A., Tsutsumi, K., Nakamura, I., Takahashi, K. and Shimamoto, Y. (2002). Structural variation around the gene encoding the α subunit of soybean β-conglycinin and correlation with the expression of the α subunit. Breed Sci. 52:285–292.
   Web of Science ®Google Scholar
• Yoshizawa, T., Shimizu, T., Yamabe, M., Taichi, M., Nishiuchi, Y., Shichijo, N., Unzai, S., Hirano, H., Sato, M. and Hashimoto, H. (2011). Crystal structure of basic 7S globulin, a xyloglucan-specific endo-beta-1,4-glucanase inhibitor protein-like protein from soybean lacking inhibitory activity against endo-beta-glucanase. FEBS J. 278:1944–1954.
   PubMed Web of Science ®Google Scholar