We investigated the chromosomal organization and developmental regulation of soybean 8-conglycinin genes. The 8-conglycinin gene family contains at least 15 members divided into two major groups encoding 2.5-kilobase and 1.7-kilobase embryo mRNAs. 8-Conglycinin genes are clustered in severa1 DNA regions and are highly homologous along their entire lengths. The two groups differ by the presence ...

BACKGROUND β-Conglycinin (conglycinin) is one of the major seed storage proteins of soybean. Conglycinin is a 7S trimer composed of different combinations of β, α and α' subunits. All subunits of conglycinin have been reported to be allergenic in humans. The goal of this research is to identify epitopes of the β subunit of conglycinin that are antigenic in multiple animal species. RESULTS Ser...

β-Conglycinin has been identified as one of the major feed allergens. However, studies of β-conglycinin on fish are scarce. This study investigated the effects of β-conglycinin on the growth, digestive and absorptive ability, inflammatory response, oxidative status and gene expression of juvenile Jian carp (Cyprinus carpio var. Jian) in vivo and their enterocytes in vitro. The results indicated...

Soybeans are recognized as one of the “big 8” food allergens. IgE antibodies from soybean-sensitive patients recognize more than 15 soybean proteins. Among these proteins only the R-subunit of -conglycinin, but not the highly homologous R′and -subunits, has been shown to be a major allergenic protein. The objective of this study was to examine if the R′and -subunits of -conglycinin can also ser...

Soy protein β-conglycinin has serum lipid-lowering and anti-obesity effects. We showed that single ingestion of β-conglycinin after fasting alters gene expression in mouse liver. A sharp increase in fibroblast growth factor 21 (FGF21) gene expression, which is depressed by normal feeding, resulted in increased postprandial circulating FGF21 levels along with a significant decrease in adipose ti...

It is well known that β-conglycinin, a soybean allergen, induces allergies and causes intestinal damage in fetuses and neonates. However, the underlying mechanisms responsible for the adverse effects of β-conglycinin remain elusive. In particular, it is unknown whether or not this dietary substance causes direct damage affecting the proliferation and integrity of intestinal cells. This study ev...

Protein quality in soybean seeds is strongly influenced by nutritional conditions. Glycinin (11S globulin) and β-conglycinin (7S globulin) are the 2 main proteins in soybean seeds. Protein quality of glycinin (11S) is higher than that of β-conglycinin (7S), due to the presence of higher amounts of s-containing amino acids (methionine and cysteine) in glycinin than β-conglycinin. Of the amino ac...

Soybean allergy presents a health threat to humans and animals. The mechanism by which food/feed allergen β-conglycinin injures the intestinal barrier has not been well understood. In this study, the changes of epithelial permeability, integrity, metabolic activity, the tight junction (TJ) distribution and expression induced by β-conglycinin were evaluated using IPEC-J2 model. The results showe...

Cereal Chem. 63(6):493-496 Quantitative analyses of soybean globulins were made by densitometry Proteins extracted with both water and 0.5M sodium chloride contained in a sodium dodecyl sulfate (SDS)-polyacrylamide slab gel using lysozyme glycinin (36.5%), /3-conglycinin (27.8%), y-conglycinin (6.2%), Kunitz as an internal standard protein and Coomassie Brilliant Blue as a staining trypsin inhi...

The degradation of the major seed storage globulins of the soybean (Glycine max [L.] Merrill) was examined during the first 12 days of germination and seedling growth. The appearance of glycinin and beta-conglycinin degradation products was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of cotyledon extracts followed by electroblotting to nitrocellulose and immunostaining...