2007
DOI: 10.1016/j.plantsci.2006.11.015
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Immunodetection and immunolocalization of tryptophanins in oat (Avena sativa L.) seeds

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Cited by 11 publications
(9 citation statements)
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“…Good foaming capacity was attributed to the absence of nonpolar lipids, the presence of a surface active lipid binding protein (tryptophanin) in water extracts from supercritical CO 2 extracted material (Kaukonen et al, 2011). Tryptophanins are tryptophane rich, low molecular weight (15 kDa), basic, and highly surface active proteins which show similarities to wheat puroindolines (Mohammadi, Zaidi, Ochalski, Tanchak, & Altosaar, 2007). As they are soluble at acidic pH environments, those highly surface active molecules could have been removed from OPI during isoelectric precipitation in the current study.…”
Section: General Discussion and Future Prospectsmentioning
confidence: 99%
“…Good foaming capacity was attributed to the absence of nonpolar lipids, the presence of a surface active lipid binding protein (tryptophanin) in water extracts from supercritical CO 2 extracted material (Kaukonen et al, 2011). Tryptophanins are tryptophane rich, low molecular weight (15 kDa), basic, and highly surface active proteins which show similarities to wheat puroindolines (Mohammadi, Zaidi, Ochalski, Tanchak, & Altosaar, 2007). As they are soluble at acidic pH environments, those highly surface active molecules could have been removed from OPI during isoelectric precipitation in the current study.…”
Section: General Discussion and Future Prospectsmentioning
confidence: 99%
“…Seed sections were blocked in 5% skim milk powder in phosphate-buffered saline/0.1% Tween (PBST) overnight at 4°C. The next morning, seed sections were incubated in a 1/100 dilution of Durotest® mouse anti-puroindoline primary antibody (R-Biopharm AG, Darmstadt, Germany) for 1 h in 2% (w/v) skim milk powder in PBST (Mohammadi et al 2007). Seed sections, still adsorbed on the surface of the glass slide, were washed for 10 min x 3 in PBST.…”
Section: Methodsmentioning
confidence: 99%
“…Wheat Guillon et al, 2004;Lovegrove et al, 2013;Philippe et al, 2006;Philippe et al, 2007); oat, rye ; barley Wilson et al, 2006;) Xylan Wheat (Lovegrove et al, 2013) Xyloglucan Wheat (Pellny et al, 2012); barley (Dwivany et al, 2009; (13),(14)--D-glucan Wheat Philippe et al, 2006); barley (Wilson et al, 2006;; maize (Carpita and McCann, 2010) Callose Wheat (Pellny et al, 2012;Philippe et al, 2006); barley (Wilson et al, 2006; Mannan Wheat (Pellny et al, 2012) (Furukawa et al, 2003;Nagamine et al, 2011;Ohdaira et al, 2011;Saito et al, 2009;Saito et al, 2008;Takahashi et al, 2005;Tian et al, 2013;Washida et al, 2009;Yasuda et al, 2009); maize (Arcalis et al, 2010;Chikwamba et al, 2003;Holding et al, 2007) Globulin Wheat (Arcalis et al, 2004); rice Tian et al, 2013); maize (Arcalis et al, 2010) Glutelin Wheat (Arcalis et al, 2004;Wang et al, 2013) Oat (Mohammadi et al, 2007) Binding protein (BiP) Rice Embryo and scutellum Dehydrin Quinoa (Carjuzaa et al, 2008) Oleosin / Caleosin Rice (Chen et al, 2012); oat (Heneen et al, 2008); barley (Liu et al, 2005) Prolamin Rice (Ohdaira et al, 2011) Cytokinin dehydrogenase Maize …”
Section: Starchy Endosperm Arabinoxylanmentioning
confidence: 99%
“…Wiley, et al (2007 provided clear evidence on the synthesis and accumulation of puroindolines by applying immunolocalization with alkaline phosphatase labeling of tissue prints. Antibodies against puroindolines and friabilin have been used to localize their counterparts in oat seed, tryptophanins, and study their changes during seed development and germination (Mohammadi, et al, 2007).…”
Section: Grain Proteinsmentioning
confidence: 99%