Results 151 to 160 of about 1,207 (175)
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Journal of Food Science, 2008
ABSTRACT: Canola is an economically important farm‐gate crop in Canada. To further explore the potential of canola protein as value‐added food and nutraceutical ingredients, a better understanding of fundamental properties of 2 major canola proteins is necessary.
J, Wu, A D, Muir
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ABSTRACT: Canola is an economically important farm‐gate crop in Canada. To further explore the potential of canola protein as value‐added food and nutraceutical ingredients, a better understanding of fundamental properties of 2 major canola proteins is necessary.
J, Wu, A D, Muir
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Plant Molecular Biology, 2015
Trafficking of seed storage proteins to protein storage vacuoles is mediated by carboxy terminal and internal sorting determinants (ISDs). Protein modelling was used to identify candidate ISDs residing near surface-exposed regions in Arabidopsis thaliana cruciferin A (AtCruA). These were verified by AtCruA fusion to yellow fluorescent protein (YFP) and
Dwayne D Hegedus, Cathy M Coutu
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Trafficking of seed storage proteins to protein storage vacuoles is mediated by carboxy terminal and internal sorting determinants (ISDs). Protein modelling was used to identify candidate ISDs residing near surface-exposed regions in Arabidopsis thaliana cruciferin A (AtCruA). These were verified by AtCruA fusion to yellow fluorescent protein (YFP) and
Dwayne D Hegedus, Cathy M Coutu
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Food Research International, 2020
The 11S globulin cruciferin is the major storage protein in Brassicaceae/Cruciferae seeds and exists as a hexamer in its natural configuration. Arabidopsis thaliana cruciferin is composed of CRUA, CRUB and CRUC subunits. Wild type (WT) cruciferin and cruciferins composed only of identical CRUA, CRUB and CRUC subunits were examined for their ability to ...
Dwayne D Hegedus +2 more
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The 11S globulin cruciferin is the major storage protein in Brassicaceae/Cruciferae seeds and exists as a hexamer in its natural configuration. Arabidopsis thaliana cruciferin is composed of CRUA, CRUB and CRUC subunits. Wild type (WT) cruciferin and cruciferins composed only of identical CRUA, CRUB and CRUC subunits were examined for their ability to ...
Dwayne D Hegedus +2 more
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Theoretical and Applied Genetics, 1995
The levels of certain essential amino acids, in particular cysteine, lysine and methionine, in the seed storage protein of a commercial spring variety of rape, Brassica napus, have been increased by the introduction of an antisense gene for cruciferin, which is the most abundant storage protein in rapeseed. The antisense construct contained part of the
J, Kohno-Murase +3 more
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The levels of certain essential amino acids, in particular cysteine, lysine and methionine, in the seed storage protein of a commercial spring variety of rape, Brassica napus, have been increased by the introduction of an antisense gene for cruciferin, which is the most abundant storage protein in rapeseed. The antisense construct contained part of the
J, Kohno-Murase +3 more
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Physiologia Plantarum, 1990
Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed (Brassica napus) during the seed development. It is composed of six subunit pairs. Each pair consists of one heavy α chain (30 kDa) and one light β chain (20 kDa). Four different subunit pairs exist.
Joakim Rödin, Lars Rask
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Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed (Brassica napus) during the seed development. It is composed of six subunit pairs. Each pair consists of one heavy α chain (30 kDa) and one light β chain (20 kDa). Four different subunit pairs exist.
Joakim Rödin, Lars Rask
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Plant Molecular Biology, 1993
The major storage protein in seeds of Brassica napus, the 12S globulin cruciferin, is composed of three different groups of subunits; cru1, cru2/3 and cru4. By using gene family-specific probes, we have investigated the accumulation, rate of synthesis and spatial distribution of transcripts corresponding to the different groups of cruciferin subunits ...
S, Sjödahl +5 more
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The major storage protein in seeds of Brassica napus, the 12S globulin cruciferin, is composed of three different groups of subunits; cru1, cru2/3 and cru4. By using gene family-specific probes, we have investigated the accumulation, rate of synthesis and spatial distribution of transcripts corresponding to the different groups of cruciferin subunits ...
S, Sjödahl +5 more
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Plant Science, 1990
Abstract Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed (Brassica napus) during seed development. It is composed of six subunit pairs. Each pair is synthesized as a precursor which in turn gives rise to one heavy α chain ( M r approx. 30 000) and one light β chain ( M r approx.
Joakim Rödin, Lars Rask
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Abstract Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed (Brassica napus) during seed development. It is composed of six subunit pairs. Each pair is synthesized as a precursor which in turn gives rise to one heavy α chain ( M r approx. 30 000) and one light β chain ( M r approx.
Joakim Rödin, Lars Rask
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SAXS and other spectroscopic analysis of 12S cruciferin isolated from the seeds of Brassica nigra
Journal of Molecular Structure, 2017Abstract Oilseeds of the plant family Brassicaceae are important for providing both lipid and protein contents to human nutrition. Cruciferins (12S globulins) are seed storage proteins, which are getting attention due to their allergenic and pathogenicity related nature.
Sven Falke, Amr Negm, Aisha Munawar
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Journal of the Science of Food and Agriculture, 1996
The heat stability of rapeseed 12S globulin (cruciferin) was examined using 8-anilinonaphthalene-1-sulphonic acid (ANS) as a fluorescence probe. Heating cruciferin (0.06-0.3 mg ml -1 in 10 mM glycyl-glycyl piperizine buffer, pH 7.0, with 0.1-1.0 M NaCl) for 20 min increased its hydrophobicity as monitored by ANS fluorescence measurements.
Yetunde L Folawiyo +1 more
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The heat stability of rapeseed 12S globulin (cruciferin) was examined using 8-anilinonaphthalene-1-sulphonic acid (ANS) as a fluorescence probe. Heating cruciferin (0.06-0.3 mg ml -1 in 10 mM glycyl-glycyl piperizine buffer, pH 7.0, with 0.1-1.0 M NaCl) for 20 min increased its hydrophobicity as monitored by ANS fluorescence measurements.
Yetunde L Folawiyo +1 more
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The behaviour of rapeseed cruciferin on chromatofocusing
Food / Nahrung, 1993AbstractCruciferin, a main storage protein of rapeseeds has been investigated by means of chromatofocusing, isoelectric focusing and electrophoresis in polyacrylamide gels. It was shown, that the half molecules of this oligomeric protein differ from each other by subunit composition. There are specific forms of cruciferin.
V. A. Reva, M. T. Kulibali
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