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  • 1
    Electronic Resource
    Electronic Resource
    Albumin storage protein and allergens in cottonseeds (1979)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 27 (1979), S. 500-503 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60223a017
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of NaCl on the in vitro Activity of Malate Dehydrogenase in Salt Marsh Halophytes of the U.S. (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 41 (1977), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The in vitro effect of NaCl on NAD-malate dehydrogenase (E.C. 1.1.1.37; MDH) from desalted extracts of roots and leaves of six salt marsh halophytes was investigated. The plants, all native and important constituents of the salt marshes of the east coast of the U.S., included Spartina alterniflora Loisel., Spartina patens (Aiton) Muhl., Distichlis spicata (L.) Greene, Juncus roemerianus Schleele, Salicornia virginica L., and Borrichia frutescens (L.) DC. In the leaf extracts of all species except Borrichia frutescens, the MDH activity was slightly stimulated by NaCl at concentrations around 0.05 M at optimal pH (8.0–8.5) and was reduced by NaCl in higher concentrations. MDH activity in the leaf extract of Borrichia frutescens was more salt-tolerant and maximal activity occurred around 0.25 M NaCl at optimal pH (7.0). Even though similar pH optimums for activity were exhibited in the root and leaf extracts of each species, the MDH activity in the root extract was more salt-tolerant than that in the leaf extract. NaCl at concentrations up to 0.1 M stimulated the MDH activity in the root extracts of all species except that of Borrichia frutescens, which had an optimal activity in 0.5 M NaCl. In the root and leaf extracts of Borrichia frutescens, the activity of cytosol MDH was much more salt-tolerant than that of the mitochondrial MDH. A shift of the optimal pH to more acidic values with increasing concentrations of NaCl was noted in the extracts of all the species except Borrichia frutescens. The action of NaCl on MDH activity appeared to be a general ionic effect as judged by the response of the enzyme activity in the presence of iso-ionic concentrations of other salts and isoosmotic mannitol. Thus, the response of the MDH from five of the salt marsh plants to NaCl is similar to that of glycophytes. However, Borrichia frutescens possesses a salt-tolerant MDH that has optimal activity in a salt concentration as high as that of the environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1977.tb01527.x
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  • 3
    Electronic Resource
    Electronic Resource
    Accumulation of proline and glycinebetaine in Spartina alterniflora Loisel. in response to NaCl and nitrogen in the marsh (1981)
    Springer
    Oecologia 49 (1981), S. 224-228 
    Details
    ISSN: 1432-1939
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The possible interaction of high soil salinity and low soil nitrogen content in affecting the growth of Spartina alterniflora Loisel in the high and low marshes of the Eastern U.S. was explored. Throughout the whole growing season, the short plants growing in the high marsh, where there was a higher soil salinity and lower available soil nitrogen, contained more proline and glycinebetaine and showed a lower leaf water potential than the tall plants growing in the low marsh. In both short and tall plants, the growing season, with the highest content occurring in spring and fall. In contrast, the glycinebetaine content in both short and tall plants remained fairly constant throughout the growing season, and was consistently at least 10 fold higher than the proline content. It is estimated that 19–30% of the total leaf nitrogen was in the form of proline and glycinebetaine in the short plants, and 14–27% in the tall plants. Ammonium nitrate fertilization in the field resulted in increased growth, higher proline and glycinebetaine contents, and lower water potentials in the short plants, but had little effect on these parameters in the tall plants. We suggest that in the low marsh, the plants can obtain sufficient nitrogen for osmoregulation and other metabolism. In the high marsh with higher soil salinity and lower nitrogen content, the plants have to allocate a even greater proportion of the already limited nitrogen supply for osmoregulation. Thus, nitrogen available for osmoregulation and other nitrogen-requiring metabolism is insufficient, resulting in reduced growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00349192
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  • 4
    Electronic Resource
    Electronic Resource
    Oleosin genes in maize kernels having diverse oil contents are constitutively expressed independent of oil contents (1996)
    Springer
    Planta 199 (1996), S. 158-165 
    Details
    ISSN: 1432-2048
    Keywords: Illinois High Oils ; Illinois Low Oils ; Oil body ; Oleosin ; Oleosin gene ; Zea (oil body)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In seeds, the subcellular storage oil bodies have a matrix of oils (triacylglycerols) surrounded by a layer of phospholipids embedded with abundant structural proteins called oleosins. We used two maize (Zea mays L.) strains having diverse kernel (seed) oil contents to study the effects of varying the oil and oleosin contents on the structure of the oil bodies. Illinois High Oils (IHO, 15% w/w oils) and Illinois Low Oils (ILO, 0.5%) maize kernels were the products of breeding for diverse oil contents for about 100 generations. In both maize strains, although the genes for oil synthesis had apparently been modified drastically, the genes encoding oleosins appeared to be unaltered, as revealed by Southern blot analyses of the three oleosin genes and sodium dodecyl sulfate-polyacrylamide gel electrophoresis with immunoblotting of the oleosins. In addition, both strains contained the same three oleosin isoforms of a defined proportion, and both accumulated oils and oleosins coordinately. Oleosins in both strains were restricted to the oil bodies, as shown by analyses of the various subcellular fractions separated by sucrosedensity-gradient centrifugation. Electron microscopy of the embryos and the isolated organelles revealed that the oil bodies in IHO were larger and had a spherical shape, whereas those in ILO were smaller and had irregular shapes. We conclude that in seeds, oleosin genes are expressed independent of the oil contents, and the size and shape of the oil bodies are dictated by the ratio of oils to oleosins synthesized during seed maturation. The extensive breeding for diverse oil contents has not altered the apparent mechanism of oil-body synthesis and the occurrence of hetero-dimer or -multimer of oleosin isoforms on the oil bodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196892
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  • 5
    Electronic Resource
    Electronic Resource
    Oleosins in the gametophytes of Pinus and Brassica and their phylogenetic relationship with those in the sporophytes of various species (1994)
    Springer
    Planta 193 (1994), S. 461-469 
    Details
    ISSN: 1432-2048
    Keywords: Brassica (oleosins) ; Gametophyte ; Oil body ; Oleosin ; Pinus (oleosins) ; Pollen ; Seed
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Oleosins, which are structural proteins on the surface of intracellular oil bodies, have been found in the sporophytic seeds of angiosperms. Here, we report an oleosin from the female gametophyte of gymnosperm Pinus ponderosa Laws, seed and another oleosin from the male gametophyte of Brassica napus L. With the pine seed gametophyte, we identified two putative oleosins of 15 and 10 kDa, which are similar to the oleosins in angiosperm seeds in terms of their presence in the oil bodies in massive quantity. The complete sequence of the cDNA encoding the gametophytic 15-kDa oleosin was obtained, and it has a predicted amino-acid sequence similar to those of oleosins in angiosperm sporophytic seeds. A Brassica napus pollen cDNA sequence, which was reported earlier, would encode an amino-acid sequence somewhat similar to those of seed oleosins. We tested if the dissimilarity signifies a substantially different oleosin in the Brassica male gametophyte or an analytic error. By direct sequencing of a polymerase chain reaction (PCR)-amplified fragment of genomic DNA, we obtained evidence showing that this reported dissimilarity is likely to have arisen from a sequencing error. Our predicted sequence of the Brassica pollen oleosin has all the structural characteristics of seed oleosins. A phylogenic tree of 20 oleosins, including those from sporophytic and gametophytic tissues of angiosperm and gymnosperm, was constructed based on their amino-acid sequences. We discuss the evolution of oleosins, and conclude that oleosins are ancient proteins with multiple lineages whose root cannot be determined at this time.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201827
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  • 6
    Electronic Resource
    Electronic Resource
    Developmental studies of NAD-malate dehydrogenase isozymes in the cotyledon of cucumber seedlings grown in darkness and in light (1976)
    Springer
    Planta 131 (1976), S. 279-284 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The total activity of NAD-malate dehydrogenase (E.C. 1.1.1.37; MDH) in the cotyledons of cucumber (Cucumis sativus L.) seeds and seedlings increased 10fold during the first 3 days of germination in darkness and then declined gradually to one third of the peak activity after 10 days. Exposure of the seedlings to light at day 3 sharply reduced the activity to one third of the peak activity within 1 day but the residual activity remained fairly constant from day 4 to day 10. In extracts of cotyledons of 2-day-old, dark-grown seedlings and of cotyledons of 6-day-old, light-grown seedlings MDH activity was resolved into 5 isozymes by starch gel electrophoresis. Three of these isozymes were identified as cytosol isozymes, one each as a mitochondrial isozyme and a microbody (glyoxysome or peroxisome) isozyme. During germination in darkness, the activities of the five isozymes increased at different rates. However, they all peaked together at day 3 and then declined gradually at a similar rate. Light applied at day 3 selectively eliminated two cytosol isozymes but did not affect the subsequent developmental pattern of the third cytosol isozyme, the mitochondrial isozyme and the microbody isozyme. Such a selective elimination of two cytosol isozymes, together with their absence in roots and green leaves, indicates that these two isozymes participate in the mobilization of food reserves during germination. The glyoxysomal and peroxisomal isozymes were not resolved in starch gel electrophoresis. Their similarities are discussed in connection with the relationship of the two enzymes and of the two types of microbodies during the greening process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385427
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  • 7
    Electronic Resource
    Electronic Resource
    Lipases in the storage tissues of peanut and other oil seeds during germination (1978)
    Springer
    Planta 141 (1978), S. 111-116 
    Details
    ISSN: 1432-2048
    Keywords: Arachis ; Cotyledons ; Germination (seeds) ; Lipases ; Oil seeds ; Seeds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The castor-bean endosperm-the best-studied material of reserve lipid hydrolysis in seed germination-was previously shown to have an acid lipase and an alkaline lipase having reciprocal patterns of development during germination. We studied oil seeds from 7 species, namely castor bean (Ricinus communis L.), peanut (Arachis hypogaea L.), sunflower (Helianthus annus L.), cucumber (Cucumis sativus L.), cotton (Gossypisum hirsutum L.), corn (Zea mays. L.) and tomato (Lycopersicon esculentum Mill.). The storage tissues of all these oil seeds except castor bean contained only alkaline lipase activity which increased drastically during germination. The pattern of acid and alkaline lipases in castor bean does not seem to be common in other oil seeds. The alkaline lipase of peanut cotyledons was chosen for further study. On sucrose gradient centrifugation of cotyledon homogenate from 3-d-old seedlings, about 60% of the activity of the enzyme was found to be associated with the glyoxysomes, 15% with the mitochondria, and 25% with a membrane fraction at a density of 1.12 g cm-3. The glyoxysomal lipase was associated with the organelle membrane, and hydrolyzed only monoglyceride whereas the mitochondrial and membrane-fraction enzymes degraded mono-, di- and triglycerides equally well. Thus, although the lipase in the glyoxysomes had the highest activity, it had to cooperate with lipases in other cellular compartments for the complete hydrolysis of reserve triglycerides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387752
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  • 8
    Electronic Resource
    Electronic Resource
    Genes encoding oleosins in maize kernel of inbreds Mo17 and B73 (1994)
    Springer
    Plant molecular biology 26 (1994), S. 1981-1987 
    Details
    ISSN: 1573-5028
    Keywords: Maize oleosin ; oil body ; oleosin gene ; oleosin isoform
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have investigated all three oleosin genes which are expressed in the kernel of maize (Zea mays L., Mo17). Oleosin genes, ole16, ole17, and ole18, encode OLE16, OLE17, and OLE18, respectively, in proportional amounts of approximately 2:1:1 in isolated oil bodies. None of the three genes has an intron or a sequence encoding an N-terminal signal peptide. The three genes are expressed coordinately during seed maturation, and their encoded oleosins are present in similar proportional amounts in oil bodies isolated from the embryonic axis, scutellum, and aleurone layer. OLE16 represents one oleosin isoform, whereas OLE17 and OLE18 are close members of another oleosin isoform. ole16 and ole18 have been mapped to single loci on chromosomes 2 (near b1 gene) and 5S (near phya2), respectively. We predict that ole17 is located on chromosome 1 (near phya1), in a chromosomal segment duplicated on chromosome 5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019508
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