Major proteins of soybean seeds. Subunit structure of .beta.-conglycinin

Thanh, Vu Huu; Shibasaki, Kazuo

doi:10.1021/jf60217a026

Cited by 234 publications

(143 citation statements)

References 8 publications

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“…Chrispeels et al [5] described 7S oligomers presumed to be trimers that were obtained from endoplasmic reticulum of developing peas and Sun et al [21] demonstrated reversible pH-dependent trimer assembly with purified phaseolin, the 7S protein in Phaseolus vulgaris that is homologous to soybean fi-conglycinin [21]. Numerous workers have reported that mature fl-conglycinin subunits are purified from seeds as trimers (reviewed in [2]), and Thanh and Shibasaki [22] describe conditions under which fl-conglycinin undergoes a reversible ionic strength-dependent dissociation from trimers to monomers, as well as a reversible association of trimers into 9S hexamers. The properties of the c¢ and fl subunits described by our results also show that assembly of trimers in vitro responds to ionic strength, although we have been unable to demonstrate an ionic strength-dependent association of trimers into hexamers.…”

Section: Discussionmentioning

confidence: 99%

Synthesis and assembly of soybean ?-conglycinin in vitro

Lelièvre

Dickinson

et al. 1992

Plant Mol Biol

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The construction of SP6-derived expression plasmids that encode normal and modified beta-conglycinin subunits is described. With the exception of an additional methionine at their NH2-terminal ends and the lack of glycans, the normal subunits synthesized at the direction of these plasmids corresponded to mature alpha and beta subunits isolated from soybean seeds. The subunits assembled into trimers in vitro that were equivalent in size to those formed in vivo. This result shows that the glycans are not required either for protein folding or oligomer assembly. Subunits produced from other plasmids, which had modifications in a highly conserved hydrophobic region in the COOH-terminal end of the subunits, either did not assemble or assembled at an extremely low rate compared to unmodified subunits. Structural changes at the more hydrophilic NH2-terminal end had mixed effects. Several subunits modified in this region assembled into trimers at rates that were either equal or greater than those for normal alpha subunits. Others assembled less completely than the normal subunits. Our results indicate that the in vitro synthesis and assembly assay will be useful in evaluating structure-function relationships in modified beta-conglycinin subunits. The results also show that structural changes at the NH2-terminal end of the subunits are tolerated to a greater extent than modifications in the hydrophobic conserved region in the COOH-terminal half of the subunits, and this information will be useful in efforts to improve soybean quality.

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Section: Discussionmentioning

confidence: 99%

Synthesis and assembly of soybean ?-conglycinin in vitro

Lelièvre

Dickinson

et al. 1992

Plant Mol Biol

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“…b-conglycinin is a trimeric glycoprotein which consists of three sub-units, a, a 0 , and b (Thanh & Shibasaki, 1978). Glycinin is a hexamer composed of an acidic (A) polypeptide linked by a disulfide bond to a specific basic (B) polypeptide (Staswick, Hermodson, & Nielsen, 1984).…”

Section: Introductionmentioning

confidence: 99%

Effect of soy protein subunit composition on tofu quality

Poysa¹,

Woodrow²,

Yu³

2006

Food Research International

135

108

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“…Because glycinin and b-conglycinin impact greatly on the nutritional value and quality of soybean products, these proteins have been studied extensively, and their primary and crystal structures have been determined (Adachi et al, 2003;Adachi, Takenaka, Gidamis, Mikami, & Utsumi, 2001;Maruyama et al, 2001;Staswick, Hermodson, & Nielsen, 1984;Thanh & Shibasaki, 1978). Glycinin is a hexamer, with a molecular mass (M r ) $ 320-380 kDa.…”

Section: Introductionmentioning

confidence: 99%