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1 d electrophoretic properties of gliadins and glutenins.
2 late in storage proteins called gliadins and glutenins.
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
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
16 ng the alpha, beta, and gamma types) and the glutenins-but gave less consistent results with the mino
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
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.
30 ion in terms of protein fractions (gliadins, glutenins) has been determined by means of RP-HPLC, to a
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
38 e that too much gliadin incorporation in the glutenin network during pasta processing tightens the pr
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
43 ), gluten index (r=0.959( * *)), and gliadin/glutenin ratio (r=-0.952( * *)), while peak II influence
45 tic dissection of the molecular basis of HMW-glutenin role in the visco-elastic properties critical f
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
54 of the protein fractions available: high MW glutenin subunits (HMW-GS) over low MW-GS, and omega-gli
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
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
62 d in omega-gliadins and low-molecular-weight glutenins that had been identified as specific targets o
64 ents were registered in the phase diagram of glutenins up to 80 degrees C, followed by partial refold
66 of the environmental triggers (gliadins and glutenins) with these gene products to trigger the immun
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