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1 d electrophoretic properties of gliadins and glutenins.
2 late in storage proteins called gliadins and glutenins.
3                             Peak I signified glutenins (30-130kDa), peak II as gliadins (20-55kDa), p
4 l) were the strongest allergens, followed by glutenins (acetic acid), albumins (water), and globulins
5 or indigenous storage proteins, gliadins and glutenins, after they too had been reduced, preferential
6 a/gamma-gliadin, high-molecular-weight (HMW) glutenin, alpha-amylase inhibitor (AAI) dimer, and wheat
7 s consist of monomeric gliadin and polymeric glutenin and determine the quality of pasta products mad
8 erwise, the orientation and order of the HMW glutenins and adjacent genes were identical in the two g
9  MW PA had greater binding affinity for both glutenins and gliadins than lower MW PA, whereas both PA
10            The thermal dependent behavior of glutenins and gliadins was analyzed through intrinsic fl
11          A higher degree of cross-linking of glutenins and of inclusion of gliadin in the polymers wa
12 igh molecular weight (HMW) subunits of wheat glutenin are major determinants of the elastic propertie
13 und that the major IgE-reactive areas of HMW glutenins are located in the repetitive regions of the p
14                                           As glutenin-bound omega-gliadins were present in wheat and
15 urea and decreased surface hydrophobicity of glutenins, but not gliadins.
16 ng the alpha, beta, and gamma types) and the glutenins-but gave less consistent results with the mino
17                 Removal of free SH groups in glutenin by adding 2.3 mumol KBrO3 or KIO3 per g dry mat
18                   The complete synthetic HMW-glutenin construct was 1908 bp, and contained 32 identic
19  alpha/beta-, gamma- and omega-types whereas glutenins contain HMW- and LMW-types.
20 s C) decreased the gliadin and increased the glutenin content.
21 l N-ethylmaleimide/g protein reduces gliadin-glutenin cross-linking during pasta drying and/or cookin
22 umol glutathione/g protein increases gliadin-glutenin cross-linking during pasta processing, resultin
23                     This first synthetic HMW-glutenin gene and future modifications are intended to a
24 ive receptor kinase gene near the y-type HMW-glutenin gene at the Glu-B1 locus is likely active as it
25 uplicate globulin gene, found 5' of each HMW-glutenin gene, assists to tentatively define the origina
26 f six genes including the two paralogous HMW-glutenin genes are disrupted in the orthologous region o
27 -type ( Glu-1-1 ) and y-type ( Glu-1-2 ) HMW-glutenin genes of the complex Glu-B1 locus were found to
28 s one of the two high-molecular-weight (HMW) glutenin genes, comprising the complex Glu-B1 locus.
29  leading to the paralogous x- and y-type HMW-glutenin genes.
30 ion in terms of protein fractions (gliadins, glutenins) has been determined by means of RP-HPLC, to a
31 lacking IgE to omega(5) -gliadin, and to HMW glutenin in 59%.
32 xhibited the known anomalous behavior of HMW-glutenins in SDS-PAGE.
33 ression of gliadins and low-molecular-weight glutenins (LMWgs) by active demethylation of their promo
34 tinct types of allelic variations at the HMW-glutenin loci in the A genomes of different hexaploid wh
35 tig covering the high molecular weight (HMW)-glutenin locus from the A genome of durum wheat (Triticu
36  macropolymers, larger size distribution for glutenin macropolymer particles and varied sodium-dodecy
37 an lower MW PA, whereas both PA precipitated glutenins more efficiently than gliadins.
38 e that too much gliadin incorporation in the glutenin network during pasta processing tightens the pr
39                     Most likely, KIO3 caused glutenin oxidation within each individual dough layer to
40 gated into five domains: peak I (130-30 kDa; glutenins), peak II (55-20 kDa; gliadins), peak III (28-
41 -1 locus, encoding the high-molecular-weight glutenin protein subunits, controls bread-making quality
42             The gene expressed the novel HMW-glutenin protein to relatively high levels in bacterial
43 ), gluten index (r=0.959( * *)), and gliadin/glutenin ratio (r=-0.952( * *)), while peak II influence
44 tained 32 identical copies of one of the HMW-glutenin repetitive domain motifs.
45 tic dissection of the molecular basis of HMW-glutenin role in the visco-elastic properties critical f
46                            Known gliadin and glutenin sequences were largely determined through cloni
47               These changes concerned mainly glutenins since beta-structures are characteristic for t
48                         During pasta drying, glutenin starts polymerizing already below 60 degrees C
49  synthetic wheat high-molecular-weight (HMW) glutenin storage protein gene analog was constructed for
50 ive abundance of three high molecular weight glutenin sub units (HMW-GS) were decreased at e[CO2].
51  called T-A-1 from the high molecular weight glutenin subunit (HMW-GS) Dx5 were measured to obtain ne
52 ted comprising a wheat high molecular weight glutenin subunit gene promoter, a 304-bp sucrose non-fer
53 substantial amounts of high-molecular-weight glutenin subunits (HMW-GS) from wheat.
54  of the protein fractions available: high MW glutenin subunits (HMW-GS) over low MW-GS, and omega-gli
55                        High-molecular-weight glutenin subunits (HMW-GS), one class of seed storage pr
56 up of gluten proteins, high molecular weight glutenin subunits (HMW-GS), plays an important role in d
57 perm, particularly the high-molecular-weight glutenin subunits (HMW-GS), which are important in deter
58         The varieties that possesses high MW glutenin subunits combinations of 91 kDa + 84 kDa + 78 k
59  for portions of high molecular weight (HMW) glutenin subunits were identified by sequence analysis o
60 quence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of ce
61 es against gliadin and high-molecular-weight glutenin subunits.
62 d in omega-gliadins and low-molecular-weight glutenins that had been identified as specific targets o
63                                 Gliadins and glutenins, the major storage proteins of wheat endosperm
64 ents were registered in the phase diagram of glutenins up to 80 degrees C, followed by partial refold
65                             The gliadins and glutenins were also reduced in vivo during germination--
66  of the environmental triggers (gliadins and glutenins) with these gene products to trigger the immun

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