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PubMed2000

Evaluating the efficacy of enzyme preparations and predicting the performance of leghorn chicks fed rye-based diets with a dietary viscosity assay.

We studied whether a single-step dietary viscosity assay could be used to evaluate the efficacy of an enzyme when added to a poultry diet. The results demonstrated a linear relationship between the log of the dietary viscosity change in vitro, as determined with the new assay and the log of the enzyme activity (xylanase) added to a rye-based diet. The sensitivity of the dietary viscosity assay was high, as little as 0.19 U of xylanase per gram of diet could be detected. In addition, there was a high correlation (r > or = 0.97; P < 0.005) between chick performance and the log of the amount of enzyme added to the diet or the log of its viscosity change in rye-based diets that contained different amounts of xylanase, as determined by the in vitro dietary viscosity assay. Further, the dose response data from the dietary viscosity assay, when incorporated into a log-linear model that we developed, was able to distinguish between the efficacy of two enzymes with regards to their ability to hydrolyze the viscosity factor in rye grain. Therefore, it was possible to accurately evaluate the efficacy of enzyme preparations in a rye diet and to predict chick performance using the new assay in conjunction with a model equation.

Animals↗
PubMed1994

A Comparison of Freezing Injury in Oat and Rye: Two Cereals at the Extremes of Freezing Tolerance.

A detailed analysis of cold acclimation of a winter rye (Secale cereale L. cv Puma), a winter oat (Avena sativa L. cv Kanota), and a spring oat cultivar (Ogle) revealed that freezing injury of leaves of nonacclimated seedlings occurred at -2[deg]C in both the winter and spring cultivars of oat but did not occur in winter rye leaves until after freezing at -4[deg]C. The maximum freezing tolerance was attained in all cultivars after 4 weeks of cold acclimation, and the temperature at which 50% electrolyte leakage occurred decreased to -8[deg]C for spring oat, -10[deg]C for winter oat, and -21[deg]C for winter rye. In protoplasts isolated from leaves of nonacclimated spring oat, expansion-induced lysis was the predominant form of injury over the range of -2 to -4[deg]C. At temperatures lower than -4[deg]C, loss of osmotic responsiveness, which was associated with the formation of the hexagonal II phase in the plasma membrane and subtending lamellae, was the predominant form of injury. In protoplasts isolated from leaves of cold-acclimated oat, loss of osmotic responsiveness was the predominant form of injury at all injurious temperatures; however, the hexagonal II phase was not observed. Rather, injury was associated with the occurrence of localized deviations of the plasma membrane fracture plane to closely appressed lamellae, which we refer to as the "fracture-jump lesion." Although the freeze-induced lesions in the plasma membrane of protoplasts of spring oat were identical with those reported previously for protoplasts of winter rye, they occurred at significantly higher temperatures that correspond to the lethal freezing temperature.

Journal Article↗
PubMed1973

Purification of oat and rye phytochrome.

A purification procedure employing normal chromatographic techniques is outlined for isolating phytochrome from etiolated oat (Avena sativa L.) seedlings. Yields in excess of 20% (25 milligrams or more) of phytochrome in crude extract were obtained from 10- to 15-kilograms lots. The purified oat phytochrome had an absorbance ratio (A(280) nm/A(665) nm) of 0.78 to 0.85, comparable to reported values, and gave a single major band with an estimated molecular weight of 62,000 on electrophoresis in sodium dodecyl sulfate-polyacrylamide gels. A modification of the oat isolation procedure was used to isolate phytochrome from etiolated rye Secale cereale cv. Balbo) seedlings. During isolation rye phytochrome exhibited chromatographic profiles differing from oat phytochrome on diethylaminoethyl cellulose and on molecular sieve gels. It eluted at a higher salt concentration on diethylaminoethyl cellulose and nearer the void volume on molecular sieve gels. Yields of 5 to 10% (7.5-10 milligrams) of phytochrome in crude extract were obtained from 10- to 12-kilogram seedling lots. The purified rye phytochrome had an absorbance ratio of 1.25 to 1.37, significantly lower than values in the literature and gave a single major band with an estimated molecular weight of 120,000 on electrophoresis in sodium dodecyl sulfate-polyacrylamide gels. It is suggested that the absorbance ratio and electrophoretic behavior of rye phytochrome are indices of purified native phytochrome, and that oat phytochrome as it has been described is an artifact which arises as a result of endogenous proteolysis during isolation. A rationale is provided for further modifications of the purification procedure to alleviate presumed protease contaminants.

Journal Article↗
PubMed1984

Fluorescence Properties Indicate that Photosystem II Reaction Centers and Light-Harvesting Complex Are Modified by Low Temperature Growth in Winter Rye.

Thylakoids isolated from winter rye (Secale cereale L. cv Puma) grown at 20 degrees C (nonhardened rye, RNH) or 5 degrees C (cold-hardened rye, RH) were characterized using chlorophyll (Chl) fluorescence. Low temperature fluorescence emission spectra of RH thylakoids contained emission bands at 680 and 695 nanometers not present in RNH thylakoids which were interpreted as changes in the association of light-harvesting Chl a/b proteins and photosystem II (PSII) reaction centers. RH thylakoids also exhibited a decrease in the emission ratio of 742/685 nanometers relative to RNH thylakoids.Room temperature fluorescence induction revealed that a larger proportion of Chl in RH thylakoids was inactive in transferring energy to PSII reaction centers when compared with RNH thylakoids. Fluorescence induction kinetics at 20 degrees C indicated that RNH and RH thylakoids contained the same proportions of fast (alpha) and slow (beta) components of the biphasic induction curve. In RH thylakoids, however, the rate constant for alpha components increased and the rate constant for beta components decreased relative to RNH thylakoids. Thus, energy was transferred more quickly within a PSII reaction center complex in RH thylakoids. In addition, PSII reaction centers in RH thylakoids were less connected, thus reducing energy transfers between reaction center complexes. We concluded that both PSII reaction centers and light-harvesting Chl a/b proteins had been modified during development of rye chloroplasts at 5 degrees C.

Journal Article↗
PubMed1980

The presence of DNA in ribosome-deficient plastids of heat-bleached rye leaves.

In leaves of rye seedlings (Secale cereale L.) grown at 32 degrees C the formation of plastid (70-S) ribosomes is specifically prevented. The resulting plastid-ribosome-deficient leaves can be used as a suitable system to identify chloroplast proteins which are translation products of cytosolic (80-S) ribosomes. The ribosome deficiency in plastids is accompanied by a bleaching of the leaves in light. In experiments aimed at finding the primary heat-sensitive event leading to ribosome deficiency the DNA of rye chloroplasts has been identified. Its properties are similar to those of chloroplast DNAs from other higher plants. The ribosome-deficient plastids isolated from heat-bleached rye leaves contained a DNA species which was indistinguishable from that of chloroplasts with regard to buoyant density in CsCl equilibrium gradients, reassociation properties and fragment patterns obtained upon cleavage by restriction endonucleases. Its quantity was comparable to that of chloroplast DNA of green leaves grown at a permissive temperature (22 degrees C). These results suggest that, unlike the effect in heat-bleached Euglena strains, lack of chloroplast DNA cannot be considered as the reason for the primary effect of high temperature in rye leaves but steps in the biosynthetic pathway of plastid ribosomes themselves must be affected more directly.

DNA↗
PubMed1994

Rye inhibitors of animal alpha-amylases show different specificities, aggregative properties and IgE-binding capacities than their homologues from wheat and barley.

Three new members of the alpha-amylase/trypsin-inhibitor family of cereal endosperm have been isolated from rye. N-terminal amino acid sequence comparison revealed that two of the purified proteins were the rye homologues of the barley monomeric inhibitor (BMAI-1) previously described, while the other rye protein corresponded to one of the subunits of the barley and wheat heterotetrameric inhibitors. However, the inhibitory specificities (active against human salivary alpha-amylase), aggregative behaviours (mainly as dimeric forms) and IgE-binding capacities (not recognized by sera from allergic patients) of the rye inhibitors were clearly different from those of their wheat and barley counterparts. These results indicate that homologous inhibitors may have distinctive properties in different cereal species.

Amino Acid Sequence↗
PubMed2001

Sources of wheat powdery mildew resistance from wheat-rye and wheat-Leymus hybrids.

Introgression of germplasm from rye and Leymus mollis has been used in the objective of broadening mildew resistance in wheat. The mildew resistant wheat lines were isolated from crosses of three hexaploid triticale lines, a mildew resistant double wheat-rye substitution line and a mildew resistant hexaploid wheat-L. mollis hybrid with three mildew susceptible breadwheats. Three different mildew isolates with a broad virulence have been used and lines with different resistance patterns, including resistance to all three mildew isolates, were selected. From a total of about 13,000 lines, eight lines from the triticale crosses, 58 from the double wheat-rye substitution line crosses and six from the L. mollis-hybrid crosses showed homozygous resistance to all three isolates. A differential tester set of wheat lines with known mildew resistance genes including earlier known resistance genes from rye showed a similarity between IRS-cultivars and the largest category in the triticale populations, indicating a higher frequency of IR chromosomes. The results are discussed in relation to the differential tester set and in relation to broadening the genetic base of resistance in wheat by interspecific hybridization.

Chimera↗
PubMed2004

Resistance genes for rye stem rust (SrR) and barley powdery mildew (Mla) are located in syntenic regions on short arm of chromosome.

Genetic stocks were developed for the localization and eventual cloning of the stem rust resistance gene SrR that occurs in wheat lines carrying the 1RS translocation from Secale cereale 'Imperial' rye. We have used a mutation-based approach for molecular analysis of the SrR region in rye. Forty-one independent mutants resulting in loss of SrR resistance were isolated: many of these were deletions of various sizes that were used to locate SrR with respect to chromosome group 1S markers. The analysis of the mutants showed that markers about 1 Mb apart flanking the barley Mla locus also flank SrR. Additionally, three of the approximately 20 closely related sequences of Mla in rye are deleted in each of six interstitial deletion mutants of SrR. The results indicate that the SrR region in rye is syntenic to the Mla region in barley or that SrR is possibly orthologous to the Mla locus.

Binding Sites↗
PubMed1977

Comparative study of rye and thymus histones: amino acid analysis and tryptic fingerprinting.

Amino acid composition and tryptic fingerprints of rye (Secal cereale) H1, H2B (PH1), and H2A(PHII) histones indicate the presence of major differences between these and the corresponding calf or rabbit fractions. In addition to variations for other amino acids, fraction H1 from rye contains twice as much arginine as the corresponding animal fraction; the plant H2B (PHI) and H2A (PHII) histones show lysine to arginine ratios greater than those of their animal counterparts. The tryptic maps of the same proteins appear to differ between plants and animals by the number and the general pattern of the peptides, as well as by the quantity and distribution of the arginine-containing peptides. Such results suggest the presence of differences in the primary structure of the calf and rye lysine-rich and moderately lysine-rich histones. Furthermore, the possibility is ruled out that each of these plant histones consists of an animal-like protein with an additional segment of 20--30 amino acid residues. On the other hand, the rye and calf arginine-rich fractions H3 and H4 show similar amino acid compositions and tryptic peptides maps.

Amino Acids↗
PubMed1984

Crossed radioimmunoelectrophoretic analysis of cultivated rye (Secale cereale) pollen allergens.

Cultivated rye pollen extracts were characterized by means of crossed immunoelectrophoresis (CIE) and crossed radioimmunoelectrophoresis (CRIE). 32 antigens were identified in CIE and among these 16 were radiostained in CRIE analysis of a rye pollen sensitive patient panel. Crossed line immunoelectrophoresis revealed that some of the rye pollen antigens were immunological partially identical with antigens of wheat flour and rye flour.

Animals↗
PubMed1985

Murine lymphocyte responses to purified components of rye grass pollen extract.

The ability of lymphocytes obtained from mice treated with whole rye grass pollen extract or purified major allergen components (R7--apparent molecular weight 31,000; R14a-apparent molecular weight 11,000) to proliferate in culture on challenge with these allergens has been studied. Whole rye grass pollen extract was found to stimulate responses with lymphocytes from all treated but not non-treated animals, whereas the purified allergens failed to effect proliferation except with cells obtained from animals treated with the homologous allergen. These results accord with previous observations that, of the antigen present in the whole rye grass pollen extract, the components showing greatest immunogenicity in murine systems are not those commonly regarded as being the major allergens in man. The mouse may not thus provide a relevant model of human immune responses to rye grass pollen extracts.

Animals↗
PubMed1988

Induction of allergen-specific T cells by conjugates of N-formyl-methionyl-leucyl-phenylalanine and rye grass pollen extract.

A conjugate of the biologically active peptide N-formyl-methionyl-leucyl-phenylalanine and rye grass pollen extract (F-MLP/rye), previously shown to react with rye grass pollen extract-specific T cells, induced the formation of allergen-specific T cells in mice. Lymph node cells prepared from mice immunized with either native extract or F-MLP/rye gave an enhanced response to unmodified rye grass pollen allergens in vitro. Syngeneic spleen macrophages were able to present the unmodified allergens to T cells obtained from both groups of mice causing their proliferation in vitro. Conjugation of the peptide into the extract brought about an extensive reduction in its reactivity with grass pollen-specific human IgE, and a loss of its ability to induce specific IgG antibody in guinea-pigs. A state of delayed hypersensitivity specific for rye grass pollen extract was produced in guinea-pigs by immunization with either the F-MLP/rye or unmodified extract. It is concluded that conjugates such as F-MLP/rye or other T' allergoids could be used as probes to investigate whether changes in T cell activity are important in immunotherapy.

Allergens↗
PubMed1988

Induction of T-helper cell activity by fragments of rye grass pollen extract produced by digestion with chymotrypsin.

Rye grass pollen extract was digested by chymotrypsin to produce fragments with a molecular weight below 10,000, as demonstrated by polyacrylamide gel electrophoresis. Chymotryptic fragments did not react with either human or mouse IgG antibodies specific for rye grass pollen, nor did they induce an antibody response in mice with specificity for the parent extract. However, macrophage-presented fragments retained the ability to react with rye-specific T cells in a lymphoproliferation assay. Furthermore, these fragments induced the development of splenocytes capable of supporting dinitrophenyl specific antibody production. This implies that the fragments still react with, and induce, rye grass pollen extract-specific T-helper cells. The possibility that such fragments might have potential for use in immunotherapy for the specific treatment of allergy is discussed.

Adjuvants, Immunologic↗
PubMed1991

Characterization of allergenic components of rye and wheat flour (Secale, Triticum vulgaris) by western blot with sera of bakers: their effects on CD23 expression.

The allergenic components of water-soluble rye flour extract were studied by immunoblotting. Sera from 100 bakers were analyzed for their IgG, IgG4 and IgE binding pattern. Two allergens with molecular weights of 35 and 14 kD were detected. Previously, the major allergens of wheat flour extract were identified. The wheat flour components at a MW of 15/17 kD and the rye flour component at a MW of 14 kD were purified and isolated. The modulation of the low affinity receptor for IgE (Fc epsilon RII/CD23) on monocytes by separated allergenic components was studied. Depending on the allergen concentration the CD23 expression on isolated cells increased after stimulation with the rye flour component (MW 14 kD). The combined addition of the rye flour component (14 kD) with IL-4 induced a significant CD23 expression as compared to IL-4 alone.

Allergens↗
PubMed2006

Rye (Secale cereale L.).

Rye (Secale cereale L.) is one of the most recalcitrant plant species for tissue culture and genetic transformation. Embryogenic rye callus loses its ability to regenerate plants quickly in response to high density of Agrobacterium and other stressors. The cocultivation of Agrobacterium and rye immature embryos in liquid medium facilitated washing of the cultures to avoid Agrobacterium overgrowth and allowed a high throughput. More than 40 independent transgenic plants were regenerated with one to four Southern-positive, independent events from 100 inoculated immature embryos. Agrobacterium strain AGL0 supported stable integration of a constitutive nptII selectable marker expression cassette into the genome of rye inbred line L22, as indicated by regeneration of plantlets on paromomycin-containing culture medium, Southern blot, Western blot, and the analysis of T-DNA::plant DNA boundary sequences. Transgenic plants were phenotypically normal and fully fertile, which might be a consequence of the short time in tissue culture.

Agrobacterium tumefaciens↗
PubMed2002

Bale compression and hydrogen phosphide fumigation to control cereal leaf beetle (Coleoptera: Chrysomelidae) in exported rye straw.

Control of larvae and adults of cereal leaf beetle, Oulema melanopus (L.), by bale compression and hydrogen phosphide fumigation was studied in rye straw, Secale cereale L., in Aurora, OR. Natural mortality of larvae after transport was 4.0 +/- 1.0% (mean +/- SEM). Compression (105 kg/cm2) of larvae in standard bales (122 cm long) of rye straw resulted in 100% mortality. Compression of adults in standard bales plus storage of the compressed bales (56 cm long) for 1 d in a freight container resulted in 100% mortality. A KD50 of 102 ppm hydrogen phosphide for 1 h was estimated from the probit regression line developed from dose-response data at 21 degrees C in basic laboratory tests. The LD50s and LD99s were 163 and 6,910 ppm for 2-h exposures and were 18 and 42 ppm for 6-h exposures at 21 degrees C, respectively. A tested close of 400 ppm for 24 h at 21 degrees C resulted in 100% mortality of the adults. Larvae (n = 10,560) and adults (n = 18,602) did not survive exposure to bale compression followed by hydrogen phosphide fumigation (60 g/28.3 m3) for 3 d in rye straw loaded in freight containers in large-scale tests. Copper plate corrosion values indicating the severity of exposure to hydrogen phosphide were 13 and 12, and mean temperatures of five locations in the freight container were 25 and 26 degrees C in large-scale tests with the larvae and adults, respectively. Hydrogen phosphide concentrations were > or = 400 ppm throughout the 3-d fumigation for larvae and during the first day of fumigation for adults. We propose that cereal leaf beetle can be controlled by a single treatment of bale compression followed by a 1-d storage period or by a fumigation in which 400 ppm hydrogen phosphide is maintained for 1 d at 21 degrees C or above. We confirmed that a multiple quarantine treatment of bale compression) followed by a 3-d fumigation will control cereal leafbeetle in exported rye straw.

Animals↗
PubMed1979

Effect of gamma irradiation, fractionation, and penicillin supplementation on the rachitogenic activity of rye for chicks.

Experiments were conducted to study the effect of gamma irradiation on the rye-vitamin D antagonism in broiler chicks. In an initial study, the irradiated grain was exposed to gamma rays for 6 hr (2 Mrad) and was fed to rachitic chicks for only 12 hr before a single oral dose of vitamin D3. In another trial, birds were fed during the entire experiment (12 days) on the different experimental diets, and the irradiated grain was exposed to gamma rays for 20 hr. Results indicate that the factor in rye that interferes with vitamin D utilization was largely inactivated by exposing this grain to gamma rays for 20 hr. Additional information is reported in this paper related to the alleviation by extraction or antibiotic supplementation on the rachitogenic properties of rye. These studies were conducted by feeding to rachitic chicks the test materials for only a short period of time (12 hr) before a vitamin D3 oral dose and measuring the bone mineralization 48 hr later. Results indicate that the rachitogenic factor in rye is not present in the ash portion of the grain, that it can be largely overcome by water extraction and penicillin supplementation, and that an organic solvent extraction has no effect. Cooked beans which depress growth and increase the growth response to antibiotics are not rachitogenic.

Animal Feed↗
PubMed1983

Effect of the addition of varied salt levels on the performance of growing chickens fed rye diets.

A series of feeding trials were conducted with Single Comb White Leghorn cockerels and broiler chickens to determine if salt per se was a contributing factor in the growth-depressing properties of rye. When added salt level increased from .3 to .6% in rye-based diets growth rate and feed conversion efficiency in young chickens improved significantly (P less than or equal to .05) but not to that of corn-fed birds. The relative growth rate of chickens fed rye diets containing .3% added salt was 78 to 86% of that of birds fed rye diets with .6% added salt.

Animals↗