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Structural features of a water-soluble L-arabino-D-xylan from rye bran.

A water-soluble L-arabino-D-xylan, obtained from the chlorite holocellulose of de-lipidated, de-starched, and de-pectinated rye bran by ammoniacal extraction, was composed of L-Ara and D-Xyl in the molar ratio 7.8:10 and had Mw 36,500 and Mn 26,950. The backbone of the polysaccharide was shown to comprise (1----4)-linked beta-D-Xylp residues, with approximately 41% unsubstituted, approximately 33% 2- or 3-substituted, and approximately 26% disubstituted. Single alpha-L-Araf groups were attached to the xylan core; only a small proportion was 2-, 3-, or 5-linked.

Carbohydrate Sequence↗

Cellular and humoral responses in coeliac disease. 2. Protein extracts from different cereals.

The humoral and cellular immune responses to grain protein extracts from coeliac-toxic and non-toxic cereals were compared by use of a number of ELISA and immunoblotting methods and the indirect leucocyte migration inhibition factor (LMIF) assay. Both adult and child coeliacs had elevated levels of serum antibody to proteins from the coeliac-toxic cereals, namely bread wheat, durum wheat, rye and barley and low levels of proteins from other cereals. Using protein blotting techniques, antibody binding was greatest to gliadins/low mol mass glutenin subunits and homologous prolamins from rye and barley, consistent with the ELISA findings. Competition ELISA and preabsorption tests indicated that antibody reaction to maize storage proteins did not simply result from cross-reaction of antigliadin antibodies. In LMIF assays, only the wheat extracts had activity in coeliac patients. This is most likely partly due to loss of some of T-cell epitopes from the extraction technique required for these proteins, as well as the relatively small effects seen for even very active fractions in the LMIF assay.

Adult↗

Quantitative analysis of the probability of intracellular ice formation during freezing of isolated protoplasts.

(i) A quantitative prediction of the temperature and cooling-rate dependence of IIF requires information on the probability distribution for IIF temperature; the super-cooling tolerance; and membrane permeability, initial cell size, Boyle-van't Hoff relation, and other parameters associated with the thermodynamic description of cell volumetric behavior. (ii) A probabilistic analysis of IIF was developed on the basis that IIF occurs if the underlying potential IIF temperature T* falls within the range of temperatures over which the cell is supercooled beyond its tolerance delta T*. The "location" of the transition range of cooling rates, in which the Pr(IIF) increases from 0 to 1, depends on the mean of T* and delta T*. The breadth of the transition range increases strongly with variability in T*. (iii) Cryomicroscopic studies of IIF in rye protoplasts isolated from cold acclimated and nonacclimated leaves showed that the range of IIF temperatures and the incidence of IIF are strongly dependent on the solute used to manipulate osmolality in the suspending medium. The ionic solutes used in this study (NaCl + CaCl2, KCl + CaCl2, KNO3 + CaCl2) generally yielded median IIF temperatures lower than those of the nonionic solutes (sucrose, sorbitol, proline). Cold acclimation reduced the median IIF temperature for all suspending media and reduced the incidence of IIF for KCl + CaCl2, sorbitol, and proline. A Weibull distribution was found to describe adequately the distribution of IIF temperatures at the highest cooling rate. (iv) Estimates of the supercooling tolerance were generally from 1.0 to 1.5 degrees C based on the location of the transition range of cooling rates and on the estimates of Lp and delta E from (6). The breadth of the transition range of cooling rates could mostly be attributed to random variability in the underlying potential IIF temperature. The rise in median IIF temperature with higher cooling rates was correctly predicted by the model when the supercooling tolerance was also assumed to be random. For rye protoplasts, both the model and the data showed that cooling-rate dependence in median IIF temperatures occurs within the transition range of cooling rates.

Edible Grain↗

Cloning and sequencing of Lol pI, the major allergenic protein of rye-grass pollen.

We have isolated a full length cDNA clone encoding the major glycoprotein allergen Lol pI. The clone was selected using a combination of immunological screening of a cDNA expression library and PCR amplification of Lol pI-specific transcripts. Lol pI expressed in bacteria as a fusion protein shows recognition by specific IgE antibodies present in sera of grass pollen-allergic subjects. Northern analysis has shown that the Lol pI transcripts are expressed only in pollen of rye-grass. Molecular cloning of Lol pI provides a molecular genetic approach to study the structure-function relationship of allergens.

Allergens↗

A major baker's asthma allergen from rye flour is considerably more active than its barley counterpart.

A rye flour protein of about 13.5 kDa, as well as its barley homologue, have been isolated. The rye component was recognized in vitro by IgE of allergic patients and provoked positive responses in 15 out of 21 baker's asthma patients (71%) when skin prick tests were performed. Its barley homologue showed no detectable in vitro reactivity and caused positive responses in only one-third of patients. Although no inhibitory activity against different alpha-amylases or trypsin was found for these two proteins, their N-terminal sequencing revealed considerable similarity to several members of the cereal alpha-amylase/trypsin inhibitor family.

Allergens↗

Effect of pollen extract on the development of experimental atherosclerosis in rabbits.

Our previous studies have shown that the pollen extract, Cernitin, reveals lipid-lowering properties in animals and humans. The present study was designed to investigate the influence of Cernitin on the development of experimental atherosclerosis in rabbits over a period of 12 weeks. Forty male mongrel rabbits were divided into 4 equal groups: (1) controls, (2) animals receiving high-fat diet (HFD) containing cholesterol and coconut oil, (3) HFD + pollen extract, and (4) HFD + clofibrate. The most pronounced reduction in lipid metabolism and in the severity of plaque formation occurred after the pollen extract had been applied. The total cholesterol content in serum and liver homogenate was depressed by 67% and 45%, respectively, while the serum HDL cholesterol and alpha-lipoproteins level was increased by 19% and from 7.73% to 21.73% respectively. The cytochrome P-450 content in the liver microsomes was elevated by 98% (nmol/g liver). Atherosclerotic plaque intensity at 12 weeks, measured planimetrically, averaged 85.5% in HFD-fed animals vs 33.7% in pollen extract-treated rabbits. These findings suggest that Cernitin, in addition to significantly lowering serum lipid levels in rabbits on an experimental diet, may modify lipid deposition in major arteries.

Animals↗

Allergenicity and cross-reactivity of rye grass pollen extracts revealed by monoclonal antibodies.

Using monoclonal antibodies the immunogenic and allergenic characteristics of rye Group I were redefined by SDS-PAGE analysis and immunoblotting. The purified rye Group I from NIH possesses a major component of approximately 34000 Da against which most of the sera from grass-sensitive patients and none from non-atopic volunteers contain specific IgE antibodies. Monoclonal antibodies to rye Group I were raised and used to purify the antigen and to verify the cross-reactivity between grass extracts. The 3 monoclonal antibodies studied recognized different components of timothy grass and 2 of them recognized kentucky june grass but none recognized components of ragweed extracts.

Allergens↗

Molecular evolution of the seed storage proteins of barley, rye and wheat.

The major storage proteins (prolamins) of barley, rye and wheat are characterized by the presence of two or more unrelated structural domains, one of which contains repeated sequences. Because of this repetitive structure and their restricted distribution (only in grasses), it has been suggested that the prolamins are of recent origin. Contrary to this hypothesis, we show that parts of the non-repetitive domain of one group of prolamins are homologous with sequences present in a large group of seed proteins from monocotyledonous and dicotyledonous plants; including Bowman-Birk protease inhibitors, cereal inhibitors of alpha-amylase and trypsin, and 2 S globulin storage proteins of castor bean and oil seed rape. This implies an ancient origin for these non-repetitive domains. The origins of the repetitive domains are not known but may lie within the grasses.

Amino Acid Sequence↗

Application of a nuclease from rye nucleus for structural studies of plant ribonucleic acids.

A new nuclease (Rn) isolated from rye nucleus was applied for the structural studies of methionine initiator transfer ribonucleic acid and ribosomal 5S rRNA from yellow lupin seeds. The enzyme shows high specificity for some regions of both RNAs. The dihydrouridine and ribothymidine loops which are supposed to be involved in the tertiary interactions of the methionine initiator tRNA were hydrolysed. The anticodon loop is not digested at all. 5S rRNA was digested in single stranded regions (loops). The cleavage pattern of the tRNA and 5S rRNA obtained with Rn enzyme, suggests not only the high specificity toward single stranded regions, but also some dependence on their tertiary structure.

Base Sequence↗

Soil to plant transfer of 239 + 240Pu, 238Pu, 241Am, 137Cs and 90Sr from global fallout in flour and bran from wheat, rye, barley and oats, as obtained by field measurements.

Crops of wheat, rye, barley and oats were grown on fields where the contamination of the soil with radionuclides resulted exclusively from global fallout debris. After machine harvesting and milling, the concentrations of 239 + 240Pu, 241Am, 137Cs and 90Sr were determined separately in bran and flour, as well as in the soils. The concentrations of 239 + 240Pu in wheat, rye and barley flour were between 59 and 180 microBq kg-1, and in oat flour 1100 microBq kg-1. The range of concentrations of the other radionuclides for the four flours were: 241Am, 5-70 microBq kg-1, 137Cs, 260-380 mBq kg-1; 90Sr, 310-1300 mBq kg-1. The corresponding concentrations of the radionuclides were always considerably higher in the bran than in the flour, with the exception of oats. The range of this factor depends on the cereal: for 239 + 240Pu, 19-25; 241Am, 10-38; 137Cs, 4-6; and for 90Sr, 4-7. Similar differences between flour and bran were observed for stable elements, for example K, Ca and Fe. The soil-to-plant transfer factors of 239 + 240Pu for wheat, rye and barley flour were between 0.00026 and 0.00078 (oats 0.017) and for bran between 0.0048 and 0.02 (oats 0.014). For 241Am the corresponding values were somewhat lower. For the wheat, rye and barley flour the transfer factors of 137Cs were between 0.013 and 0.018 (oats 0.069) and, for the bran, between 0.08 and 0.10 (oats 0.16). The corresponding values for 90Sr were significantly higher: for flour between 0.08 and 0.14 (oats 1.2) and for bran between 0.62 and 0.93 (oats 1.5).

Americium↗

The regional distribution of selenium in Greek cereals.

The selenium content of hard and soft wheat, barley, oats, rye and corn grown in approximately 100 different locations of Greece has been determined fluorimetrically. The mean values +/- SD for these cereal types were 0.29 +/- 0.19, 0.21 +/- 0.12, 0.16 +/- 0.10, 0.14 +/- 0.10, 0.19 +/- 0.10 and 0.12 +/- 0.08 ppm Se (dry weight basis), respectively. Based on data for selenium in corn from 96 different locations, a geobotanic map of Greece for the selenium in soil available for uptake by plants was prepared. Macedonia, West Epirus, south-east Thessaly, north-east Sterea Hellas and the Aegean Islands produce corn deficient or low in selenium, but only sporadic selenium-deficiency diseases in animals have been observed in many of these areas, probably because the farm animals are given mixed food or they are free to graze. No areas with toxic levels of selenium in soil were found.

Edible Grain↗

In vivo detection of genotoxicity in waste water from a wheat and rye straw paper pulp factory.

The genotoxicity of waste water from a wheat and rye straw paper pulp mill was investigated by in vivo genotoxicity tests using micronuclei and sister chromatid exchange as endpoints. Micronuclei were studied in mussels (Mytilus edulis) and sister chromatid exchange in fish (Nothobranchius rachowi). The paper mill uses chlorine dioxide for bleaching, and the bleaching effluent as well as the combined effluent, i.e. the mixture of all waste water streams, were both tested. Both effluents induced micronuclei and sister chromatid exchanges, although the presence of toxic substances could mask the expression of genotoxicity in some cases for both test systems. The study revealed that genotoxins are produced in the chlorine dioxide bleaching process as well as in the pulping process, indicating also genotoxic activity of non-chlorinated compounds. In contrast to previous studies in which mutagenicity was determined with bacterial assays, genotoxins were only associated with chlorinated organics from bleaching with chlorine and failed in detecting genotoxins in chlorine dioxide bleaching effluents. Aquatic in vivo genotoxicity tests are sensitive and efficient systems and seem to be a promising tool in effluent testing.

Animals↗