Structural and Functional Analysis of Various Globulin Proteins from Soy Seed

Critical Reviews in Food Science and Nutrition

Volumn 55, Issue 11, 2015, Pages 1491-1502

  Singh, Amandeep ^a   Meena, Megha ^a   Kumar, Dhiraj ^a   Dubey, Ashok K ^a   Hassan, Md Imtaiyaz ^b  

^a NETAJI SUBHAS INSTITUTE OF TECHNOLOGY   (India)

^b JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

Author keywords

11S and 7S globulin; basic 7S globulin; hypo cholesterolemic effect; Soybean globulins; Conglycinin

Indexed keywords

AMINO ACIDS; CHAINS; COVALENT BONDS; GENES; OLIGOMERS; PROTEINS;

11S AND 7S GLOBULIN; BASIC 7S GLOBULINS; CONGLYCININ; HYPO-CHOLESTEROLEMIC EFFECT; SOYBEAN GLOBULINS;

BIOSYNTHESIS;

GLYCINE MAX;

BETA-CONGLYCININ PROTEIN, GLYCINE MAX; GLOBULIN; GLYCININ; PLANT ANTIGEN; SEED STORAGE PROTEIN; SOYBEAN PROTEIN;

AMINO ACID SEQUENCE; CHEMISTRY; PLANT SEED; SOYBEAN;

AMINO ACID SEQUENCE; ANTIGENS, PLANT; GLOBULINS; SEED STORAGE PROTEINS; SEEDS; SOYBEAN PROTEINS; SOYBEANS;

EID: 84926434233     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408398.2012.700340     Document Type: Article

References (112)

1. 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.
2. 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.
3. 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.
4. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. 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.
11. Catsimpoolas, N. (1968). Micro isoelectric focusing in polyacrylamide gel columns. Anal. Biochem. 26:480–482.
12. 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.
13. Catsimpoolas, N. and Ekenstam, C. (1969). Isolation of alpha, beta, and gamma conglycinins. Arch. Biochem. Biophys. 129:490–497.
14. 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.
15. 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.
16. Chen, A. and Shoemaker, R. (1998). Four genes affecting seed traits in soybeans map to linkage group F. J. Hered. 89:211–215.
17. 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.
18. Cho, T. J. and Nielsen, N. C. (1989). The glycinin Gy3 gene from soybean. Nucleic Acids Res. 17:4388.
19. Chrispeels, M. J. (1991). Sorting of proteins in the secretory system. Annu. Rev. Plant Phys. 42:21–53.
20. 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.
21. 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.
22. 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.
23. 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.
24. Derbyshire, E., Wright, D. J. and Boulter, D. (1976). Legumin and vicilin, storage proteins of legume seeds. Phytochem. 15:3–24.
25. 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.
26. Dickinson, C. D., Hussein, H. E. and Nielsen, N. C. (1989). Role of posttranslational cleavage in glycinin assembly. Plant cell 1(4):459–469.
27. 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.
28. 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.
29. 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.
30. 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.
31. Ereken-Tumer, N., Richter, J. D. and Nielsen, N. C. (1982). Structural characterization of the glycinin precursor. J. Biol. Chem. 257:4016–4018.
32. 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.
33. 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.
34. Fischer, R. L. and Goldberg, R. B. (1982). Structure and flanking regions of soybean seed protein genes. Cell 29:651–660.
35. 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.
36. 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/
37. 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.
38. Geldberg, R. B. (1986). Regulation of plant gene expression. Philos. Trans. R. Soc. Lond B Biol. Sci. 314:11.
39. 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.
40. Goldberg, R. B. and Sims, T. L. (1989). The glycinin Gy1 gene from soybean. Nucleic Acids Res. 17(11):4386.
41. 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.
42. Hara-Nishimura, I. and Nishimura, M. (1987). Proglobulin processing enzymes in vacuoles isolated from developing pumpkin cotyledons. Plant Phys. 85:440–455.
43. 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.
44. 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.
45. 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.
46. Hirano, H., Kagawa, H. and Okubo, K. (1992). Characterization of proteins released from legume seeds in hot water. Phytochem. 31:731–735.
47. 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.
48. Hofmann, K., Bucher, P., Falquet, L. and Bairoch, A. (1999). The Prosite database, its status in 1999. Nucleic Acids Res. 27:215–219.
49. Holm, L. and Rosenstrom, P. (2010). Dali server: conservation mapping in 3D. Nucleic Acids Res. 38(Suppl. 2):W545–W549.
50. 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.
51. 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.
52. Kagawa, H., and Hirano, H. (1989). Sequence of a cDNA encoding soybean basic 7S globulin. Nucleic Acids Res. 17:8868.
53. 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.
54. Kambara, H., H. M., Takamatsu, K. and Kito, M. (2002). Triglyceride-lowering effect of soybean b-conglycinin in humans. Ther. Res. 23:85–89.
55. 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.
56. 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.
57. Kinsella, J. (1979). Functional properties of soy proteins. J. Am. Oil Chem. Soc. 56:242–258.
58. 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.
59. 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/
60. Koshiyama, I. (1965). Purification of the 7S component of soybean proteins. Agric. Biol. Chem. 29:3.
61. Koshiyama, I. (1968a). Chemical and physical properties of a 7S protein in soybean globulins. Cereal. Chem. 10.
62. Koshiyama, I. (1968b). Factors influencing conformation changes in a 7S protein of soybean globulins by ultracentrifugal investigations. Agric. Bioi. Chern. (Tokyo) 9.
63. Koshiyama, I. and Fukushima, D. (1976a). Identification of the 7S globulin with β-conglycinin in soybean seeds. Phytochem. 15:157–159.
64. Koshiyama, I. and Fukushima, D. (1976b). Purification and some properties of γ-conglycinin in soybean seeds. Phytochem. 15:161–164.
65. 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.
66. 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.
67. 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.
68. 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.
69. 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.
70. 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.
71. 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.
72. 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.
73. 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.
74. 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.
75. 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.
76. Meinke, D. W., Chen, J. and Beachy, R. N. (1981). Expression of storage-protein genes during soybean seed development. Planta 153:130–139.
77. 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.
78. Nicholas, C. (1969). Isolation of glycinin subunits by isoelectric focusing in urea-mercaptoethanol. FEBS Lett. 4:259–261.
79. Nielsen, N. C. (1984). The chemistry of legume storage proteins. Philos. Trans. Roy. Soc. London B, Biol. Sci. 304:287–296.
80. Nielsen, N. (1985). The structure and complexity of the 11S polypeptides in soybeans. J. Am. Oil Chem. Soc. 62:1680–1686.
81. 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.
82. 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.
83. 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.
84. 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.
85. 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.
86. ′ and β-subunits of the soybean 7S seed storage protein. Nucleic Acids Res. 10:8245–8261.
87. 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.
88. 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.
89. 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.
90. Sirtori, C. R. and Lovati, M. R. (2001). Soy protein and cardiovascular disease. Curr. Atheroscler. Rep. 3(1):47–53.
91. 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.
92. 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.
93. 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.
94. Thant, V. H., Turner, N. E. and Nielsen, N. C. (1989). The glycinin Gy2 gene from soybean. Nucleic Acids Res. 17:4387.
95. Tombs, M. P. (1967). Protein bodies of the soybean. Plant Phys. 42:797–813.
96. 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.
97. 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.
98. 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.
99. 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.
100. Vu Huu, T. and Shibasaki, K. (1978). Major proteins of soybean seeds. Subunit structure of.beta.-conglycinin. J. Agr. Food Chem. 26:692–695.
101. ′- and α-subunits. Plant Phys. 158:1395–1405.
102. 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.
103. Watanabe, Y. and Hirano, H. (1994). Nucleotide sequence of the basic 7S globulin gene from soybean. Plant Phys. 105:1019–1020.
104. 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.
105. Wolf, W. T. T. (1969). Heat denaturation of soybean 11S protein. Cereal Chem. 46:14.
106. 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.
107. 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.
108. 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.
109. 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.
110. 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.
111. 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.
112. 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.