Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “soybean”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 127 records · Page 7Linked to original sources
PubMedDate not supplied

Genetic study of a lethal necrosis to soybean mosaic virus in PI 507389 soybean.

PI 507389 soybean [Glycine max (L.) Merr.], a large-seeded line from Japan, exhibits a rapid, lethal, necrotic response to strains G1, G2, G5, and G6 of soybean mosaic virus (SMV). Unlike the hypersensitive necrotic reaction, this stem-tip necrosis can be a serious threat to soybean production. To investigate the genetic basis of lethal necrosis (LN), PI 507389 was crossed with the susceptible (S) cv. Lee 68 and with resistant (R) lines PI 96983, cv. York, and cv. Marshall, which carry single dominant genes for SMV resistance at the Rsv1 locus. F(1) plants, F(2) populations, and F(2:3) lines were inoculated with G1 and G6 in the greenhouse or in the field. Results indicated that LN is controlled by a single gene allelic to Rsv1, and this allele in PI 507389 is recessive to R alleles in PI 96983, York, and Marshall. The LN allele is codominant with the allele for S, for the heterozygotes showed a mixed phenotype of both necrosis (N) and mosaic (M) symptoms (NM). The LN allele becomes recessive to the S allele as the mixed NM shifts to S at a later stage in response to more virulent strains. The gene symbol Rsv1-n is assigned for the allele conferring LN in PI 507389. Rsv1-n is the only allele at the Rsv1 locus conditioning N to G1 and no R to any other SMV strains, and thus a unique genotype for SMV strain differentiation. The phenotypic expression of heterozygotes and the dominance relationships among R, N, and S depend on the virulence of SMV strains, source of alleles, and developmental stage.

Alleles↗
PubMed1999

Hydrogen gas production of broiler chicks in response to soybean meal and alpha-galactoside free, ethanol-extracted soybean meal.

In order to measure broiler chick hydrogen gas production, a sealed atmosphere chamber was constructed and chicks were intubated with soybean meal (SBM), alpha-galactoside free, ethanol-extracted soybean meal (ESBM), and ESBM with alpha-galactosides added to the levels of SBM (ESBMG). Six male broiler chicks averaging 156 g of weight were deprived of feed for 12 h prior to intubation with 6 g of the test soybean meals. Two chicks were used for each treatment. Following intubation, chicks were placed in the sealed atmosphere chamber for 20 min at 2-h intervals for 28 h. At the end of this 20-min period, a sample of the chamber atmosphere was collected with a gas-tight syringe and analyzed for hydrogen gas by gas-solid chromatography. The hydrogen production of the two chicks intubated with SBM peaked 7 h postintubation at 127 ppm. The ESBM produced a peak at approximately 17 h postintubation at 26 ppm. Intubation with ESBMG resulted in peak hydrogen production at approximately 12 h postintubation at an average of 67 ppm. Results indicate that chicks intubated with SBM produced 3.2 times the amount of total hydrogen gas than those chicks intubated with ESBM. Chicks intubated with ESBMG produced 2.2 times the amount of total hydrogen gas than chicks intubated with ESBM. The research indicates the alpha-galactoside oligosaccharides are a major cause of hydrogen gas production from SBM in poultry.

Animal Feed↗
PubMed1997

A G-Box-Binding Protein from Soybean Binds to the E1 Auxin-Response Element in the Soybean GH3 Promoter and Contains a Proline-Rich Repression Domain.

The E1 promoter fragment (-249 to -203) is one of three auxin-response elements (AuxREs) in the soybean (Glycine max L.) GH3 promoter (Z.-B. Liu, T. Ulmasov, X. Shi, G. Hagen, T.J. Guilfoyle [1994] Plant Cell 6: 645-657). Results presented here further characterize and delimit the AuxRE within the E1 fragment. The E1 fragment functioned as an AuxRE in transgenic tobacco (Nicotiana tabacum L.) plants, as well as in transfected protoplasts. The AuxRE within E1 contains a G-box, and this G-box was used to clone a G-box-binding factor (GBF) from soybean (SGBF-2). This 45-kD GBF contains an N-terminal proline-rich domain and a C-terminal basic/leucine zipper DNA-binding domain. Gel-mobility shift assays were used to characterize the binding specificity of SGBF-2. Antiserum raised against recombinant SGBF-2 was used to further characterize SGBF-2 and antigenically related GBFs in soybean nuclear extracts. Co-transfection assays with effector and reporter plasmids in carrot (Daucus carota L.) protoplasts indicated that the N-terminal proline-rich domain of SGBF-2 functioned as a repression domain in both basal and auxin-inducible transcription.

Journal Article↗
PubMed1983

Effect of supra-ambient oxygen on nitrogenase activity (c(2)h(2)) and root respiration of soybeans and isolated soybean bacteroids.

Isolated soybean (Glycine max [L.] Merr. cv Wilkin) bacteroids have O(2)-dependent nitrogenase activity which is strongly inhibited by supraoptimal O(2) concentrations. Oxygen-inhibited nitrogenase activity is recovered by addition of 10 millimolar sodium succinate or by lowering the O(2) concentration.Brief treatment of roots of intact soybean plants with 1.0 atmosphere O(2) reduces nitrogenase activity (C(2)H(2)). There is a rapid partial recovery of activity within 2 to 3 hours, and a slower return to near normal levels by 36 hours. The drop and recovery of nitrogenase activity is accompanied by a parallel drop and increase in root respiration. There is a direct relationship between the change in respiration and the change in acetylene reduction following O(2) treatment. The O(2)-mediated changes in nitrogenase activity and root respiration are not affected by the planting medium. The ratio of the change in respiration to the change in nitrogenase activity was the same in 13 soybean cultivars.

Journal Article↗
PubMed1990

Sugar metabolism in germinating soybean seeds: evidence for the sorbitol pathway in soybean axes.

Characterization of sugar content and enzyme activity in germinating soybean (Glycine max L. Merrell) seeds led to the discovery of sorbitol accumulating in the axes during germination. The identity of sorbitol was confirmed by relative retention times on high-performance liquid chromatography and gas liquid chromatography and by mass spectra identical with authentic sorbitol. Accumulation of sorbitol in the axes started on day 1 of germination as sucrose decreased and glucose and fructose increased. Sucrose also decreased in the cotyledons, but there was no accumulation of sorbitol, glucose, or fructose. Accumulation of sorbitol and hexoses was highly correlated with increased invertase activity in the axes, but not with sucrose synthase and sucrose phosphate synthase activities. Sucrose synthase activity was relatively high in the axes, whereas the activity of sucrose phosphate synthase was relatively high in the cotyledons. Ketose reductase and aldose reductase were detected in germinating soybean axes, but not in cotyledons. Fructokinase and glucokinase were present in both axes and cotyledons. The data suggest a sorbitol pathway functioning in germinating soybean axes, which allows for the interconversion of glucose and fructose with sorbitol as an intermediate.

Journal Article↗
PubMed1991

Glyceollin I in soybean-cyst nematode interactions : spatial and temporal distribution in roots of resistant and susceptible soybeans.

Accumulation of the phytoalexin glyceollin I in roots of soybean (Glycine max [L.] Merr.) following inoculation with race 1 of Heterodera glycines Ichinohe, the soybean cyst nematode (SCN), was determined in a whole-root system by high performance liquid chromatography (HPLC) and in a cross-section system by a radioimmunoassay procedure. In the whole-root system, roots were harvested from controls and nematode-inoculated seedlings immediately after inoculation and at 2-day intervals for 8 days. The roots were extracted with ethanol, and the extracts were subjected to HPLC. Glyceollin I was not detected in roots of either resistant cultivar Centennial or susceptible cultivar Ransom immediately after inoculation with SCN but steadily accumulated in large quantity in roots of Centennial. Accumulation of glyceollin I in roots of Ransom following nematode inoculation was minimal. In the cross-section system, 3-day-old soybean seedlings were inoculated with juvenile nematodes, and root segments containing a single nematode were dissected from inoculated plants at 4-hour intervals under a dissecting microscope. The root segments were embedded in ice and cut into 16-micrometer sections with a cryostat microtome. The spatial and temporal distribution of glyceollin I was determined with a radioimmunoassay procedure specific for the phytoalexin. Glyceollin I was found to accumulate in tissues immediately adjacent to the head region of the nematode in Centennial but not in Ransom. Glyceollin I was detected 8 hours after nematode penetration, and the concentration increased steadily up to 0.3 micromole per milliliter in Centennial 24 hours after penetration.

Journal Article↗
PubMed2006

In vivo measurement of flatulence and nutrient digestibility in dogs fed poultry by-product meal, conventional soybean meal, and low-oligosaccharide low-phytate soybean meal.

OBJECTIVE: To determine an optimal window for determining peak flatulence and evaluate the effects of oligosaccharides and supplemental beta-mannanase in soybean meal-based diets on nutrient availability and flatulence. ANIMALS: 6 dogs. PROCEDURES: Dogs were used in a 2 x 3 factorial arrangement of treatments in a 6 x 6 Latin square experiment to evaluate the digestibility, flatulence, and fecal odor metabolites of low-oligosaccharide low-phytate soybean meal (LLM), conventional soybean meal (SBM), and poultry by-product (PBP) meal diets with or without supplemental beta-mannanase (5 g/kg). RESULTS: Enzyme supplementation had no effect on total tract dry matter (DM), nitrogen digestibility, or digestible energy; however, differences between protein sources did exist for total tract DM digestibility and digestible energy. The PBP meal had higher DM digestibility and digestible energy (mean, 0.913 and 4,255 cal/g), compared with soy-based diets (mean, 0.870 and 4,049 cal/g). No differences were detected for any treatment regardless of protein source or addition of supplemental enzyme for any flatulence components analyzed. No differences were detected for all fecal odor metabolites regardless of addition of supplemental enzyme; however, differences between protein sources were detected. The PBP meal had lower concentrations of carboxylic acids and esters and higher concentrations of heterocycles, phenols, thio and sulfides, ketones, alcohols, and indoles than LLM and SBM. CONCLUSIONS AND CLINICAL RELEVANCE: Diets containing < 22.4 g of stachyose/kg and < 2 g of raffinose/kg did not alter digestibility or increase flatulence in dogs.

Animal Feed↗
PubMed2004

Ileal amino acid digestibilities by pigs fed soybean meals from five major soybean-producing countries.

Growing conditions and processing technologies to which soybeans (SB) are exposed have an effect on digestibilities of AA found in the resultant soybean meals (SBM). This study evaluated SBM from five major SB-producing countries (Argentina, Brazil, China, India, and the United States). An industry representative in each country collected samples of unprocessed SB and SBM subjectively determined to be of high, intermediate, or low quality. The SB from each country were processed into SBM under uniform conditions in the United States. Five experiments (each examining the three SBM and the SB processed in the United States from a single country) were conducted to determine true ileal AAd digestibilities. In addition, a standard SBM purchased on the open market in the United States was used in all experiments as a control. Data from pigs fed a low-protein casein diet in each study were used to calculate true AA digestibilities. Pigs were fitted with simple T-cannulas at the terminal ileum and allotted to treatments in Latin square design experiments. Duplicate experiments were conducted at the University of Illinois and at The Ohio State University. Within each country comparison, pigs fed the SBM processed in the U.S. from SB grown in the five countries had lower (P < 0.05) true total amino acid (TAA) digestibilities than did pigs fed any of the SBM prepared within the country of origin, except the United States. This indicates that processing conditions used at the U.S. pilot plant were not ideal when using SB from other countries. True TAA digestibilities of the diets containing the high-, intermediate-, and low-quality SBM did not differ, except for China, where the low-quality SBM (83.5%) had a lower (P < 0.05) digestibility than the intermediate- (89.6%) or high- (89.0%) quality meals. Soybean meal produced in Argentina (average, 87%) and Brazil (average, 82%) had lower (P < 0.05) true TAA digestibilities than did the standard SBM (91%), indicating that the processing plants in those countries may produce a less digestible SBM than that available on the open market in the United States.

Agriculture↗
PubMed2000

[Primary identification of organic compounds in soybean rhizospheric soil on continuous and alternate cropping and their allelopathy on soybean seed germination].

Organic compounds extracted with ethanol (OCEWE) from soybean rhizospheic soil on continuous and alternate cropping at pod-string were identified by gas chromatography-mass spectrometry (GC-MS). The results showed the compounds mainly include organic acids, alcohol, acetone, aldehyde, naphthalene phenyl and furan hydrocarbon, many of which were reported as allelochemcals. Under this experiment condition, OCEWE did not show any allelopathy on soybean seed germination and radicle growth, which might be related with their critical toxicity concentrations. In addition, the relationship between allelopathy and barrier on soybean continuous and alternate cropping was also discussed.

Acids↗
PubMedDate not supplied

[Distribution of soybean mosaic virus antigen in the leaves of soybean plants with different reaction to virus infection].

The distribution and accumulation of soybean mosaic virus antigen in the leaves of sensitive plants with well expressed mosaic symptoms and symptomless tolerant soybean plants Glycine max (L.) Merr. were similar. Low concentration of virus antigen was found in extremely resistant soybean plants in mechanically inoculated leaves and those of the 2-4 circles two-three weeks after inoculation but 5 weeks later the virus antigen was detected only in the top leaves.

Antigens, Viral↗
PubMed2006

[Construction of RNAi binary vector of soybean receptor-like kinase gene (rlpk2) and its soybean transformation].

Plant receptor-like kinases (RLKs) play important roles in plant growth, development and responses to environmental stress. RNA interference (RNAi) is a powerful tool to study functions of RLKs. In this study, a 312bp 3'end cDNA fragment of the soybean receptor-like kinase gene rlpk2 was chosen to construct the rlpk2-RNAi expression cassette. The binary vector pART27-R2 harboring rlpk2-RNAi expression cassette was constructed through three times subcloning via mid-clone vector and then transformed into Agrobacterium LBA4404. Three independent transgenic plants were obtained by Agrobactium-mediated soybean cotyledon transformation method. RT-PCR analysis showed that rlpk2 gene was successfully knocked down in all transgenic plants. It was found that photosynthesis activities of rlpk2-RNAi transgenic leaves were much improved, suggesting rlpk2 may function as a negative regulator of soybean leaf functions and/or chloroplast structure.

Gene Expression Regulation, Plant↗
PubMed1977

Studies on soybean trypsin inhibitors. XI. Complete amino acid sequence of a soybean trypsin-chymotrypsin-elastase inhibitor, C-II.

Soybean inhibitor C-II, which inhibits trypsin, alpha-chymotrypsin, and elastase, was reduced and S-carboxymethylated, and digested with trypsin. The amino acid sequences of the resulting tryptic peptides were determined by conventional methods, establishing the complete 76-amino acid sequence of the inhibitor. Inhibitor C-II was found to be homologous with soybean (Glycine max) Bowman-Birk inhibitor and more closely related to an inhibitor from garden beans (Phaseolus vulgaris). The homology with these inhibitors and the limited proteolysis of C-II indicated the reactive sites of C-II for elastase and trypsin to be alanine-22 and arginine-49, respectively. Arginine-49 was also identified as a reactive site for alpha-chymotrypsin. It was found that only a few replacements of one or two amino acid residues around the reactive sites resulted in considerable alteration of the inhibitory specificity.

Amino Acid Sequence↗
PubMed1978

Studies on soybean trypsin inhibitors, XII. Linear sequences of two soybean double-headed trypsin inhibitors, D-II and E-I.

Soybean inhibitor D-II is an inhibitor of bovine trypsin. Sequence analysis was carried out on the reduced and S-carboxymethylated protein by conventional methods to establish the complete amino acid sequence. The sequence of D-II indicated high homology with other legume inhibitors, but it was unique because of the occurrence of identical residues (arginine) at both of the reactive sites. This structure is thought to reflect that of a prototype double-headed inhibitor. The possible evolutionary process of the legume double-headed inhibitors is discussed on this basis. Comparison with another soybean inhibitor C-II suggested that a single methionine (C-II)-glutamine (D-II) replacement at the P2'position resulted in the loss of alpha-chymotrypsin inhibitory activity of D-II. The results of a hydrogen peroxide oxidation experiment on C-II supported this suggestion. The sequence of the amino-terminal 21 residues of inhibitor E-I was determined using a sequentor. It was shown that this inhibitor lacks the amino-terminal nine residues of D-II.

Amino Acid Sequence↗
PubMed2000

Protein and energy evaluation of soybean meals processed from genetically modified high-protein soybeans.

A conventional and two genetically modified soybean samples were processed to dehulled soybean meal (SBM) at a pilot plant and were compared with SBM from a commercial processing plant. Crude protein levels (%) of the experimental SBM samples were M700, 52.5; M702, 53.4; and M703, 62.7. The commercial SBM sample (UI) contained 47.5% protein. Amino acid, gross energy, lipid, and fiber analyses were carried out, and true metabolizable energy and true amino acid digestibility were determined with adult cecectomized cockerels. Digestible Lys, Met, Cys, Thr, and Val, and also TMEn, were higher (P < 0.05) and NDF, fat, and phospholipids were lower in M703 than in the other SBM samples. The results of this study indicate that M703 has considerable advantages over conventional SBM as a feed ingredient for broiler chickens.

Amino Acids↗
PubMed2003

Investigating the possibility of monitoring lectin levels in commercial soybean meals intended for poultry feeding using steam-heated soybean meal as a model.

Native soybean lectins (SBL) could potentially have deleterious effects on young animals. The objectives of this study were to determine the optimum processing temperature and time at which SBL is inactivated and to investigate the possibility of using urease activity (UA) to predict residual lectin levels in soybean meal (SBM). Raw defatted SBM was steam-heated at incremental temperatures between 90 and 120 degrees C for 5 to 20 min in an autoclave. The processed meals were subjected to native-PAGE and measurement of total carbohydrate-binding lectin (TCBL), agglutinating lectin (AL), UA, and trypsin inhibitor (TI). Processing severity was evaluated by determining protein solubility in 0.2% potassium hydroxide. Results indicated that levels of all antinutrients (TCBL, AL, UA, and TI) decreased with increasing processing temperature (P < 0.05). The intensity of the lectin band on the electrophoresis gel was considerably reduced when meal was heated at 100 degrees C for 5 min. This result implied that lectin inactivation occurred at 100 degrees C. More than 90% of all the original antinutrient levels in the raw meal were destroyed when meals were heated at 100 degrees C for 5 min. Meals processed at 100 degrees C for 5 to 20 min had protein solubility values (80 to 85%) indicative of adequate processing. The denaturation pattern of UA was highly correlated with that of SBL (r > or = 0.73), indicating that UA could be used for monitoring lectin levels in commercial meals. We concluded that UA of 0.03 to 0.09 units of pH change are indicative of adequately processed meals that contain negligible lectin levels.

Animal Feed↗
PubMed2006

Interaction of native Bowman-Birk soybean protease inhibitor and its hydrophobized derivative with multilamellar vesicles of soybean phospholipids.

The interaction of native Bowman-Birk soybean protease inhibitor (BBI) and its hydrophobized derivative with multilamellar vesicles of various soybean phospholipids was investigated. Decrease in pH and introduction of negatively charged components to the lipid mixture increased BBI content in the protein-lipid complex. This suggests a contribution of electrostatic forces in the protein-lipid interaction. Protein hydrophobization insignificantly influenced BBI binding to lipids. In the complex with lipids, both proteins (BBI and its hydrophobized derivative) retained high anti-chymotrypsin activity (75-100%), which was not influenced by the presence of the ionic detergent sodium deoxycholate.

Deoxycholic Acid↗
PubMed2004

Genetic characterization of a novel Tib-derived variant of soybean Kunitz trypsin inhibitor detected in wild soybean (Glycine soja).

A novel variant of soybean Kunitz trypsin inhibitor (SKTI) was detected in 530 lines of wild soybean (Glycine soja). This variant showed an intermediate electrophoretic mobility between the Tia and Tic types. In isoelectric focusing polyacrylamide gel electrophoresis gels containing urea, this variant had a similar isoelectric point as that of Tia. The genetic analysis of SKTI bands in F2 seeds from crosses of the new variant type with Tia or Tic type showed that this variant type is controlled by a codominant allele at the SKTI locus. We propose the genetic symbol Tif for this novel variant. When the nucleotide sequence of the Tif gene was compared with those of other types of SKTI genes (Tia, Tib, and Tic), the sequence of Tif was identical to that of Tib with the exception of one A-->G transitional mutation occurring at position 676 of Tif. This mutation resulted in an amino acid change from Lys to Glu at the 178 residue. These results suggest that this variant is derived from Tib through a point mutation. In addition, we settled an inconsistency in the number of amino acid differences between Tia and Tib (eight or nine). Analysis of nucleotide and amino acid sequences revealed that Tib was different from Tia by nine amino acids.

Amino Acid Sequence↗
PubMed2005

Oligomerization endows enormous stability to soybean agglutinin: a comparison of the stability of monomer and tetramer of soybean agglutinin.

Soybean agglutinin is a tetrameric legume lectin, each of whose subunits are glycosylated. This protein shows a very high degree of stability when compared to the other proteins of the same family. In a previous work, it was shown that the unusual stability of the protein is due to a high degree of subunit interactions. In this study we present the thermodynamic parameters for the stability of soybean agglutinin monomer. The monomeric species is found at pH 2 and below which it is most populated at pH 1.9, as evident from size-exclusion chromatographic and dynamic light scattering studies. The analyses of circular dichroism and fluorescence spectroscopy suggest that the monomer is well folded, and that it has certain characteristic features when compared to its tetrameric counterpart. The conformational stabilities of the tetramer and the monomer at the temperature of their maximum stabilities (310 K) are 59.2 kcal/mol and 9.8 kcal/mol, respectively, indicating that oligomerization contributes significantly to the stability of the native molecule. Also, the T(g) difference for the two forms of the protein is approximately 40 K, whereas the difference in DeltaC(p) is only 1.6 kcal/mol/K. This suggests that the major hydrophobic core is present in the monomer itself, and that oligomerization involves mainly ionic interactions.

Biophysical Phenomena↗