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At least 19 recordsLinked to original sources
PubMed1987

Fructose 2,6-bisphosphate in germinating oat seeds. A biochemical study of seed dormancy.

When dormant oat seeds were imbibed at the non-permissive temperature of 30 degrees C, the concentration of phosphoenolpyruvate and of glycerate 3-phosphate, which are two inhibitors of phosphofructokinase 2, increased almost linearly during 30 h. By contrast, these metabolites increased only after a lag period of about 10 h in non-dormant seeds imbibed at the same temperature. As a consequence of this, the concentration of the C3 derivatives remained always remarkably lower in non-dormant than in dormant seeds. Accordingly, the concentration of fructose 2,6-bisphosphate, which increased similarly in the two types of seeds during the first 8 h after the start of inhibition, then reached a plateau in dormant seeds but continued to increase for another 8 h in non-dormant seeds, reaching a maximal value a few hours before the beginning of radicle protrusion. When the dormant seeds were imbibed at the permissive temperature of 10 degrees C, the evolution of all metabolites was slowed down but behaved like that of non-dormant seeds imbibed at 30 degrees C. Experiments in which the dormant seeds were submitted to a jump from 10 degrees C to 30 degrees C and vice versa, always provoked reverse changes in the concentration of the C3 derivatives and of fructose 2,6-bisphosphate, the latter being increased in all conditions that allowed germination. Dormant seeds were also allowed to germinate at 30 degrees C by imbibition during 24 h in the presence of 3% ethanol. Again, this permissive treatment caused an arrest in the accumulation of C3 derivatives and an increase in fructose 2,6-bisphosphate. Another, apparently unrelated, biochemical difference between dormant and non-dormant oat seeds was their inorganic pyrophosphate content, which was approximately five-fold higher in non-dormant than in dormant seeds. This difference was observed before and persisted during imbibition as long as measurement could be made and was not affected by the temperature jumps or by ethanol. In contrast to the phosphoric esters under investigation, pyrophosphate was not preferentially located in the embryo.

Edible Grain↗
PubMed1992

Early embryo invasion as a determinant in pea of the seed transmission of pea seed-borne mosaic virus.

Seed transmission of an isolate of pea seed-borne mosaic virus (PSbMV) in several pea genotypes has been studied. Cross-pollination experiments showed that pollen transmission of PSbMV did not occur and accordingly, virus was not detected in pollen grains by ELISA or electron microscopy. Comparative studies between two pea cultivars, one with a high incidence of seed transmission and one with none, showed that PSbMV infected the floral tissues (sepals, petals, anther and carpel) of both cultivars, but was not detected in ovules prior to fertilization. Virus was detected equally well in seed coats of the progeny in both cultivars. Analysis of virus incidence and concentration in pea seeds of different developmental stages demonstrated that in the cultivar with a high incidence of seed transmission, PSbMV directly invaded immature embryos, multiplied in the embryonic tissues and persisted during seed maturation. In contrast, the cultivar without seed transmission did not show invasion of immature embryos by the virus; there was no evidence for virus multiplication or persistence during embryo development and seed maturation. Hence seed transmission of PSbMV resulted from direct invasion of immature pea embryos by the virus and the block to seed transmission in the non-permissive cultivar probably occurred at this step.

Blotting, Northern↗
PubMed1992

Accumulation of a Brazil nut albumin in seeds of transgenic canola results in enhanced levels of seed protein methionine.

We have increased the methionine content of the seed proteins of a commercial winter variety of canola by expressing a chimeric gene encoding a methionine-rich seed protein from Brazil nut in the seeds of transgenic plants. Transgenic canola seeds accumulate the heterologous methionine-rich protein at levels which range from 1.7% to 4.0% of the total seed protein and contain up to 33% more methionine. The precursor of the methionine-rich protein is processed correctly in the seeds, resulting in the appearance of the mature protein in the 2S protein fraction. The 2S methionine-rich protein accumulates in the transgenic seeds at the same time in development as the canola 11S seed proteins and disappears rapidly upon germination of the seed. The increase in methionine in the canola seed proteins should increase the value of canola meal which is used in animal feed formulations.

Gene Expression↗
PubMed1977

[Nutritive-physiological study of sunflower seed protein isolate and spun sunflower seed protein-casein fibers].

Compared with defatted sunflower seeds, in sunflower seed globulin isolates the content of lysine and sulphur containing amino acids is decreased, the content of phenylalanine is increased. The content of the whole essential amino acids of sunflower seed globulin isolate in relation to casein is decreased. The value of the enzymatic invitro available amino acids of sunflower seed globulin is comparable with casein. The digestibility is good, the biological value is in relation to defatted sunflower seed lower. Apart from the lower content of sulphur-containing amino acids the amino acid composition of spun sunflower seed globulin/casein (I:I) fibers corresponds with the calculated value; in relation to sunflower seed globulin isolate the content of lysine and the whole essential amino acids of the spun protein fibers is increased. The enzymatic in-vitro-hydrolysis results altogether in a comparable availability of the amino acids between spun protein fibers and sunflower seed globulin isolates. The digestibility and the biological value of spun protein fibers corresponds with that of casein.

Amino Acids↗
PubMed1983

Mechanism of the increase in cytochrome c oxidase activity in pea cotyledons during seed hydration. The presence of free cytochrome-c-oxidase subunits in dry cotyledons and their probable assembly into the holoenzyme during seed hydration.

The increase in cytochrome c oxidase activity in pea cotyledons during seed hydration was investigated with two kinds of antibodies against the enzymes purified from mitochondria of pea shoot and sweet potato root. The antibody against the pea enzyme recognized only the largest of the enzyme subunits (subunit I), while that against the sweet potato one did other three of the pea enzyme subunits: the second largest (subunit II) and the two smallest (subunits IV and V). There was no increase in the amount of protein immunoprecipitated with the anti-(pea enzyme) antibody in a crude fraction of cotyledon membranes during seed hydration, despite the marked increase in cytochrome c oxidase activity. Neither cycloheximide nor chloramphenicol had any effect on the activity or the amount. The crude membrane fraction from dry cotyledons contained an enzymatically inert protein precipitated with the anti-(pea enzyme) antibody. The inert protein could be separated from the active enzyme protein through solubilization of the protein from the membranes with various concentrations of Triton X-100. It consisted of only one kind of polypeptide with the same molecular weight as subunit I and decreased with the concomitant increase in the active enzyme protein during seed hydration. Dry pea cotyledons also contained a soluble protein that was immunoprecipitated by antibody to the sweet potato enzyme. The soluble form of the immunoreactive protein decreased with the concomitant increase in active cytochrome c oxidase protein in the crude membrane fraction from the cotyledons during seed hydration. None of these changes during seed hydration were inhibited by cycloheximide or chloramphenicol. The soluble, immunoreactive protein contained only one kind of polypeptide, of which the molecular weight was identical to that of subunit IV. The mitochondrial inner membranes of dry cotyledons were separated into three fractions by sucrose density gradient centrifugation. The lightest was the richest of the three in the enzymatically inert protein immunoprecipitated with the anti-(pea enzyme)antibody; cytochrome c oxidase activity in this fraction increased immediately after the onset of seed hydration. These results indicate that a membrane-bound, free form of subunit I and a soluble, free form of subunit IV of cytochrome c oxidase exist in dry pea cotyledons. We propose that these free forms of subunits are assembled with the other subunits to form the active cytochrome c oxidase during seed hydration.

Electron Transport Complex IV↗
PubMed1990

Nutritive value of rubber seed (Hevea brasiliensis) meal: utilization by growing pigs of semipurified diets in which rubber seed meal partially replaced soybean meal.

Thirty-six four-way cross (Chester White X Landrace X Large White X Yorkshire) growing barrows and gilts were used to investigate the effects of replacing graded levels of protein from soybean meal with equivalent levels of protein from rubber seed meal in 16% CP semipurified diets on the performance characteristics, hematocrit, plasma metabolites and N utilization of pigs. The first diet (control) was largely cornstarch-soybean meal in which the soybean meal supplied all of the CP. In other diets, rubber seed meal replaced 10%, 20% and 30%, respectively, of the protein of soybean meal in the control diet. Twenty gilts were used in a 28-d growth trial and 16 barrows were used in an 8-d digestion trial (4-d collection). There were no differences (P greater than .05) in ADG, ADF intake and in the feed:gain ratios, even though there was a trend for lower ADG and gain:feed ratio as the level of rubber seed meal increased in the diet. There were no differences in hematocrit, but plasma protein and albumin tended to be depressed when rubber seed meal provided more than 10% of the dietary protein. Apparent digestibilities of GE, DM and N were lower with rubber seed meal at 20% of the protein than with any other diet, but apparent N retained and the percent of digested N retained were not depressed significantly (P greater than .05). Although rubber seed meal protein is of poorer quality than soybean meal protein for growing pigs, at least 10% of dietary protein can be provided by rubber seed meal without adversely affecting growth and N utilization.

Animal Feed↗
PubMed2025

ODR1, the key seed dormancy and germination regulator, promotes seed Proanthocyanidin biosynthesis via interaction with TTG1 and modulation of MBW complex activity.

Seed dormancy and germination are crucial for both plant survival and reproduction and for crop sowing and harvesting. Proanthocyanidins (PAs), one of the most abundant seed metabolites, play a role in enhancing dormancy and inhibiting germination. Multiple regulatory factors involved in PAs biosynthesis can alter seed dormancy or germination capacity. However, whether the dormancy or germination factors reciprocally influence the PAs biosynthesis is unclear. Here, we report that ODR1, a seed dormancy and germination key factor and a transcriptional (co-) repressor, can regulate seed PAs biosynthesis and act as a transcriptional co-activator. The odr1 mutant shows lighter seed coat color, decreased PAs contents, and reduced expression of PAs biosynthesis genes, which are restored in the ODR1 complementary lines. ODR1 interacts with TTG1 and forms a complex with TTG1/TT2/TT8 (three MBW complex components), enhancing their activation on promoters of PAs biosynthesis genes like DFR and ANS. Overexpressing TTG1 in the odr1-2 mutant rescues or even reverses PA-related phenotypes of odr1-2, confirming that ODR1-mediated regulation of PAs biosynthesis is dependent on TTG1. Moreover, three homologous copies of ODR1 in rapeseed were identified, and simultaneous knockout of them reduces the PAs contents. These results revealed the previously uncharacterized functions of ODR1 in PAs biosynthesis, suggested its conservation between Arabidopsis and rapeseed, and provided important gene resources for rapeseed variety improvement.

Proanthocyanidins↗
PubMed1975

[Isothiocyanate and vinyl thio-oxazolidone contents of rape seeds and rape seed oil].

Comparative studies on the isothiocyanate content of rape-seeds and rape-seed oil show that, apart from nearly 300 mg/100 g of vinyl thio-oxazolidone, rape-seeds contain almost 200--300 mg/100 g of isothiocyanates of which 3-butenyl isothiocyanate and 4-pentenyl isothiocyanate (ratio of 4:1) are the main components as evidenced thin-layer and gaschromatographically. Only about 1 mg/100 g of isothiocyanates are found in pressed rape-seed oil; and but circa 10 mg/100 g, in extracted rape-seed oil. 3-Butenyl isothiocyanate and 4-pentenyl isothiocyanate (ratio of 4:1) are once more the main components. Thioglycerides are not detected in the oil. Vinyl thio-oxazolidone is found only in extracted rape-seed oil (about 2 mg/100 g).

Chromatography, Gas↗
PubMed1977

[Contamination of cotton seeds and of cotton seed cake by aflatoxin].

Following the discovery of aflatoxin M in cow's milk in the previous study, the contamination with aflatoxin of cotton-seed and cotton-seed cake which constitute the principal feed of local animals was measured. The samples were taken from 2 factories. The grain from the 1st factory was grown in the centre of the country in dry climate, and those from the 2nd source originated from the humid region of the north of Iran. The grain and cotton-seed cake from the 1st factory did not contain aflatoxin before storage. During storage the sample contamination amount and percent increased with time in both regions, with the dry less than the humid. In conclusion, Iranian cotton-seed and cotton-seed cake appear to be contaminated with aflatoxin B in 2 processes. The 1st is aflatoxin contamination before harvest, in the humid region of Iran; the 2nd is general storage aflatoxin contamination in both regions in which humidity and length of storage appear to be the principal factors.

Aflatoxins↗
PubMed1990

Survey of the mycoflora and mycotoxins of cotton seeds and cotton seed products in Egypt.

Thirty-nine species and 16 fungal genera were isolated from Egyptian cotton seeds, cotton seed meal and cotton seed cake on 1% glucose-Czapek's agar medium incubated at 28 degrees C. Aspergillus was the most frequent genus and it emerged in 87-100% of the samples contributing 70-98% of total fungi in the three substrates tested. The most common species were A. niger, A. flavus, A. fumigatus, A. terreus and Rhizopus stolonifer; A. niger, A. fumigatus and Penicillium corylophilum; and A. niger, A. flavus, A. terreus, A. nidulans and Rhizopus stolonifer, respectively. Cotton seeds and cotton seed products were naturally contaminated by aflatoxin B1 and B2. About 16% of the different substrates tested were positive for aflatoxin contamination. No citrinin, ochratoxin A, patulin, sterigmatocystin, diacetoxyscirpenol, T-2 toxin or zearalenone were detected in the samples assayed.

Aspergillus↗
PubMedDate not supplied

Integration of enzyme-linked immunosorbent assay with conventional chromatographic procedures for quantitation of aflatoxin in individual cotton bolls, seeds, and seed sections.

Integration of an enzyme-linked immunosorbent assay (ELISA) with conventional chromatographic methods proved the versatility of ELISA as a research tool and allowed for rapid assessment of aflaxtoxin in individual cottonseeds, parts of cottonseed, and composite samples of seeds taken from individual cotton bolls. Aqueous acetone was substituted for methanol in the extraction procedure prescribed by ELISA. The substitution allowed the use of a common extract for all analytical methods. An aliquot of the extract was used to screen samples by ELISA. Negative samples were identified, and toxin levels between 1 and 70 ng/g were quantitated by ELISA. Samples with toxin levels beyond the upper limit of detection by ELISA were then subjected to more time-consuming conventional cleanup prior to quantitation by liquid chromatography (LC) or thin-layer chromatography (TLC). Toxin levels detected by LC or TLC ranged from 100 to 845,000 ng/g sample. The screen by ELISA detected large numbers of toxin-negative cotton bolls or individual seeds in minimum analysis time. The combination of techniques verified the presence of seed with no toxin adjacent to toxin-containing seed in the same lock. Toxin-negative portions of individual seed with high toxin in another portion were identified for the first time. Integration of techniques provided needed information on distribution patterns of aflatoxin in cotton so that preventive measures can be developed.

Aflatoxin B1↗
PubMed1989

A jack bean protein similar to pea seed ferritin and unrelated to concanavalin A is the only iron storage protein in jack bean seeds, although concanavalin A can form ferritin-like iron cores in vitro.

Iron storage in living organisms is performed by ferritins. These proteins are built up from 24 subunits organized in a spherical shell forming a coat to a core of bioavailable iron. Recently, it was observed that concanavalin A from jack bean can form in vitro iron cores similar to those of animal ferritins (Yariv, J., Kalb, A. J., Helliwell, J. R., Papiz, M. Z., Bauminger, E. R., and Nowik, I. (1988) J. Biol. Chem. 263, 13508-13510). From this observation and from the comparison of the three-dimensional structures of horse spleen ferritin and of the form of concanavalin A which forms soluble polynuclear iron complexes, these authors suggested that concanavalin A is the apoferritin of jack bean seeds. On the basis of immunological and biochemical results, we report here that a protein purified from jack bean seeds, unrelated to concanavalin A and similar to plant seed ferritins, is responsible for iron storage in jack bean seeds. Furthermore, concanavalin A does not contain iron in vivo. Therefore we conclude that a unique protein, ferritin, stores iron in vivo in jack bean seeds and that concanavalin A provides an unusual model for studying the formation of iron cores inside a protein shell.

Amino Acids↗
PubMed1992

Differential manifestation of seed mortality induced by seed-specific expression of the gene for diphtheria toxin A chain in Arabidopsis and tobacco.

A pea vicilin promoter-diphtheria toxin A (DTx-A) chain gene fusion was introduced into Arabidopsis and tobacco. The chimeric Dtx-A gene behaves as a dominant, seed-lethal, Mendelian factor, and the segregation ratios are consistent with the numbers of integrated copies as revealed by Southern blotting. Germination deficiency results from distinct developmental abnormalities, thus allowing genetic dissection of seed development. The endosperm is affected first in both species. In Arabidopsis, full cellularization of the initially syncytial endosperm does not take place, which results in shrinkage and a shriveled appearance of the mature dry seed. The embryo, which appears structurally normal and lacks visible lesions, ceases to develop at the partially recurved cotyledon stage and does not use the remaining endosperm. In tobacco, peripheral degeneration and premature termination of cellular endosperm development occurs at the cotyledon initiation stage. Lesions appear in the cotyledons at the advanced cotyledon stage, but the embryo continues to grow and attains nearly the same size and level of differentiation as mature wild-type embryos before degeneration and intracellular disintegration take place throughout. Accumulation of protein bodies and other cytoplasmic inclusions is very limited and occurs only in few cells. The timing and distribution of lesions follow a pattern typical for accumulation of protein bodies in wild-type seeds. These observations are consistent with expression of the vicilin promoter in the enlargement phase of cell differentiation. A novel tissue interaction arises, when the embryo uses up all the arrested endosperm: the embryo proves to be capable of absorbing the parenchyma layers of the integument, which are normally obliterated by, and incorporated into, the endosperm.(ABSTRACT TRUNCATED AT 250 WORDS)

Arabidopsis↗
PubMed1986

[Cadmium in blue poppy seeds and poppy seed-containing products].

Blue poppy seeds, semi finished products and finished baked goods with poppy seeds, were analyzed for cadmium by atomic-absorption spectrometry. The average content was 0.739 mg/kg (median 0.654 mg/kg) for poppy seeds, 0.317 mg/kg (median 0.366 mg/kg) for semi finished products and 0.107 mg/kg (median 0.088 mg/kg) for baked goods. Poppy seeds therefore must be considered as one of the most cadmium contaminated foods. For consumers, especially children, recommendations for consumption should be established.

Cadmium↗
PubMed1977

Modification of the radiosensitivity of barley seed by post-treatment with caffein. IV. Effect of the moisture content of seed and storage temperature after irradiation.

The oxygen-dependent damage which develops in barley seeds with approximately 7-8 per cent moisture content disappears after post-irradiation storage in vacuo for 48 hours at 40 degrees C and for 24 hours at 50 degrees C. When the diration of storage at 40 degrees C is extended to 384 hours, oxygen-independent damage becomes potentiated. There is oxygen-dependent damage in seeds of approximately 13.3 per cent moisture content and after the seeds have been stored in vacuo at 50 degrees C, the oxygen-dependent damage begins to increase by 168 hours, and it is very significantly potentiated by 192 hours. Under these circumstances, caffeine acts as a radioprotector only as long as the precursors of oxic damage are present in the seeds. Once these sites are lost, caffeine acts only as a radiosensitizer. The oxygen-independent damage which increases with storage at high temperature is further potentiated by caffeine.

Caffeine↗
PubMed1991

Characterization of 2S seed storage protein of Brassica campestris and its antigenic homology with seed proteins of other Cruciferae.

The low molecular weight seed storage protein of Brassica campestris has been isolated and its amino acid composition determined. Antibody raised against this low molecular weight protein has been used to compare the antigenic similarity between the low molecular weight storage proteins of different Cruciferae seeds by immunoprecipitation and Western blotting. These studies revealed the existence of antigenically homologous proteins of identical molecular weights in seeds of other Cruciferae but absent in some other dicots like mung bean and tobacco seeds.

Amino Acids↗