Identification of peptides in blood following oral administration of ß-conglycinin to Wistar rats.

In this study, ß-conglycinin (100 mg/kg) was orally administered to Wistar rats in order to identify peptides that may be derived from the protein in the blood. Plasma samples taken from the tail vein up to 8 h after administration were analyzed by matrix-assisted laser desorption/ionization (MALDI) and liquid chromatography-time-of-flight (LC-TOF) mass spectrometry (MS). In total, 126 signals were detected by MALDI-MS. Among the signals, nine oligopeptides (SEL, KGPL, SILGA, DSEL, GDANI, SYFV, CLQSC, GEQPRPF, and LVINEGDA) were successfully identified as ß-conglycinin-derived peptides by LC-TOF/MS at a plasma concentration of 0.75-756 pmol/mL. The results demonstrated that ß-conglycinin could be the dietary source protein for the oligopeptides produced prior to entering the circulating bloodstream of rats.

The dynamic process of dietary soybean ß-conglycinin in digestion, absorption, and metabolism among different intestinal segments in grass carp (Ctenopharyngodon idella).

The present study aimed to investigate the dynamic process of soybean ß-conglycinin in digestion, absorption, and metabolism in the intestine of grass carp (Ctenopharyngodon idella). Fish fed with 80 g ß-conglycinin/kg diet for 7 weeks, the intestinal digestive enzyme was extracted to hydrolyze ß-conglycinin in vitro, the free amino acid and its metabolism product contents in intestinal segments were analyzed. The present study first found that ß-conglycinin cannot be thoroughly digested by fish intestine digestive enzyme and produces new products (about 60- and 55-kDa polypeptides). The indigestible ß-conglycinin further caused the free amino acid imbalance, especially caused free essential amino acid deficiency in the proximal intestine but excess in the distal intestine. Moreover, these results might be partly associated with the effect of ß-conglycinin in amino acid transporters and tight junction-regulated paracellular pathway. Finally, dietary ß-conglycinin increased the content of amino acid catabolism by-product ammonia while decreased the amino acid anabolism product carnosine content in the proximal intestine and distal intestine. Thus, the current study first and systemically explored the dynamic process of ß-conglycinin in digestion, absorption, and metabolism, which further supported our previous study that dietary ß-conglycinin suppressed fish growth and caused intestine injure.

Characterization of the antigenic specificity of soybean protein beta-conglycinin and its effects on growth and immune function in rats.

The objective of the present study was to characterize the antigenic specificity of purified soybean beta-conglycinin and to investigate its effects on the growth and immune responses of rats. Thirty-two Brown Norway rats, 3 weeks of age, were randomly allotted to one of four treatments and individually fed casein-cornstarch based diets. Rats were sensitised by means of intragastric gavage with purified beta-conglycinin (0, 5, 10 or 20 mg protein/ml in phosphate buffered saline at pH 7.4) on day 0, 7, 14, and 21 (1 ml/animal). On day 28, rats received a double dose of beta-conglycinin. Blood was obtained at weekly intervals after initiation of challenge. Growth declined linearly with increasing the concentration of soybean beta-conglycinin (p < 0.05). Both the total IgE and beta-conglycinin-specific IgE levels in serum increased while passive cutaneous anaphylactic reactions were induced in the rats. Lymphocyte proliferation response to concanavalin A in plasma and spleen was increased linearly with increased levels of soybean (p < 0.01) beta-conglycinin. The percentage of CD4+ lymphocyte subset linearly increased (p < 0.001). As a result, the concentrations of cytokines in plasma and spleen, including interleukin-4 (p < 0.01), interleukin-5 (p < 0.01), and tumour necrosis factor-alpha (p < 0.01) increased linearly with increasing level of purified beta-conglycinin. Our results indicate that purified beta-conglycinin possesses intrinsic immune-stimulating capacity and can induce an allergic reaction. Therefore, dietary soybean beta-conglycinin has negative effects on growth and both cell-mediated and humoral immune function in rats.

Inhibitory effect of a soybean-protein--related moiety on iron absorption in humans.

The inhibitory effect of soybean protein isolates on nonheme-iron absorption was studied in 34 human subjects. Iron absorption was measured by using an extrinsic radioiron label in liquid-formula meals containing hydrolyzed corn starch, corn oil, and either egg white or a series of soybean-protein derivatives. The unmodified soybean-protein isolate markedly inhibited iron absorption. Percentage absorption was 19-fold higher when an extensively enzyme-hydrolyzed preparation with very little phytate was used as the protein source. Both the glycinin (11S) and conglycinin (7S) fractions of soybean protein were inhibitory to iron absorption. Dephytinization removed the inhibitory effect of the glycinin but not of the conglycinin fraction. We conclude that there are two major inhibitors of iron absorption in soybean-protein isolates, phytic acid and a protein-related moiety contained in the conglycinin (7S) fraction.

Immunologic, clinical, and pathologic aspects of human graft-versus-host disease.

The three necessary factors in the development of graft-versus-host disease are the histoincompatibility of the host and the effector cells of this process, the immunoincompetence of the host, and the capability of effector cells to proliferate and attack host tissues protractedly in vivo. The disease may affect the alimentary tract, liver, bronchopulmonary tree, bone marrow, reticuloendothelial system, vascular endothelial cells, or epidermis. Graft-versus-host disease is potentially reversible or controllable if prompt, aggressive therapy is instituted. The recommended treatment is a combination of methotrexate, high-dose prednisone, and antithymocyte globulin.