2001
DOI: 10.1006/jcrs.2001.0380
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Albumin and Globulin Proteins of Wheat Flour: Immunological and N-terminal Sequence Characterisation

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Cited by 36 publications
(28 citation statements)
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“…Spot 3 corresponds to the cleavage of proglobulin-3A at cleavage site 3, with predicted M r 28.6 kDa and pI 5.76. The processing of Spot 4 is supported by N-terminal sequence data that matches the previously documented cleavage site 2 (XXHGDSRR) [26]. Spot 4 corresponds to cleavage of proglobulin-3A at cleavage sites 2 and 4, with predicted M r 35.1 kDa and pI 9.14.…”
Section: Resultssupporting
confidence: 73%
See 1 more Smart Citation
“…Spot 3 corresponds to the cleavage of proglobulin-3A at cleavage site 3, with predicted M r 28.6 kDa and pI 5.76. The processing of Spot 4 is supported by N-terminal sequence data that matches the previously documented cleavage site 2 (XXHGDSRR) [26]. Spot 4 corresponds to cleavage of proglobulin-3A at cleavage sites 2 and 4, with predicted M r 35.1 kDa and pI 9.14.…”
Section: Resultssupporting
confidence: 73%
“…These findings suggest that these ~30 kDa globulin-3-related polypeptides could arise from different processing events of the same precursor, as was observed for barley Beg1 [9,35]. Curiously, there were no proteins identified in the immunoblotting experiments that corresponded to the product of processing at cleavage site 4, as was documented in other studies that sequenced globulin-3 (Figure 3 and [19,20,26]). Potentially, as the anti‐globulin-3A antibodies are polyclonal and were prepared by the co-immunization of rabbits with a mixture of two separate peptides [45], it is possible that the antibodies recognize only one of the two peptides.…”
Section: Discussionsupporting
confidence: 68%
“…Analysis of sequence coverage indicated that these spots were produced by cleavage of the N-termini of these proteins. These results are consistent with previous investigations indicating that globulin-3 family proteins can be processed at internal cleavage sites to yield polypeptides with a large range of molecular weights and pI values (Singh et al 2001;Dupont et al 2011;Koziol et al 2012). Interestingly, the spots corresponding to full-length globulin were downaccumulated under e[CO 2 ], whereas those corresponding to endo-proteolytic events accumulated or appeared in samples grown under these conditions.…”
Section: Changes In Seed Proteome Profilessupporting
confidence: 92%
“…Variation of subunits between gliadin and glutenin proteins in mealy/vitreous kernels can affect the Gli-to-Glu ratio, which is an important indicator of grain technological/baking quality. In our study it varied between cultivar samples from 1.08 to 1.31, and was similar to that presented by Singh et al (2001), Shewry and Halford (2002), Konopka et al (2007), and Gil-Humanes et al (2012). According to Samson et al (2005), the Gli-to-Glu ratio of vitreous endosperm in durum wheat was higher than 0.85 in more than 98% of the samples.…”
Section: Discussionsupporting
confidence: 48%