ライフサイエンスコーパス: glutenin

1 h strength in the order of LMW-GS < gluten < glutenin.

2 gories of gliadins and high molecular weight glutenins.

3 d electrophoretic properties of gliadins and glutenins.

4 late in storage proteins called gliadins and glutenins.

5 in; but also, soluble glutenin and insoluble glutenin (1:1).

6 Peak I signified glutenins (30-130kDa), peak II as gliadins (20-55kDa), p

7 ine lowered gliadin and low-molecular-weight glutenin accumulation by 50% to 60% and increased free a

8 l) were the strongest allergens, followed by glutenins (acetic acid), albumins (water), and globulins

9 or indigenous storage proteins, gliadins and glutenins, after they too had been reduced, preferential

10 a/gamma-gliadin, high-molecular-weight (HMW) glutenin, alpha-amylase inhibitor (AAI) dimer, and wheat

11 s consist of monomeric gliadin and polymeric glutenin and determine the quality of pasta products mad

12 ween gliadin and glutenin; but also, soluble glutenin and insoluble glutenin (1:1).

13 ructure of dough by the inclusion of gluten, glutenin and LMW-GS, which lacks resemblance among diffe

14 base flour dough by the addition of gluten, glutenin and purified low molecular weight glutenin subu

15 erwise, the orientation and order of the HMW glutenins and adjacent genes were identical in the two g

16 MW PA had greater binding affinity for both glutenins and gliadins than lower MW PA, whereas both PA

17 The thermal dependent behavior of glutenins and gliadins was analyzed through intrinsic fl

18 high screw speed caused the insolubility of glutenins and globulins while increasing the solubility

19 A higher degree of cross-linking of glutenins and of inclusion of gliadin in the polymers wa

20 igh molecular weight (HMW) subunits of wheat glutenin are major determinants of the elastic propertie

21 und that the major IgE-reactive areas of HMW glutenins are located in the repetitive regions of the p

22 5-30%, whereas weak flours had 16% insoluble glutenin, as a percentage of flour protein.

23 As glutenin-bound omega-gliadins were present in wheat and

24 urea and decreased surface hydrophobicity of glutenins, but not gliadins.

25 ng the alpha, beta, and gamma types) and the glutenins-but gave less consistent results with the mino

26 our had balance not only between gliadin and glutenin; but also, soluble glutenin and insoluble glute

27 Removal of free SH groups in glutenin by adding 2.3 mumol KBrO3 or KIO3 per g dry mat

28 The complete synthetic HMW-glutenin construct was 1908 bp, and contained 32 identic

29 alpha/beta-, gamma- and omega-types whereas glutenins contain HMW- and LMW-types.

30 s C) decreased the gliadin and increased the glutenin content.

31 l N-ethylmaleimide/g protein reduces gliadin-glutenin cross-linking during pasta drying and/or cookin

32 umol glutathione/g protein increases gliadin-glutenin cross-linking during pasta processing, resultin

33 This first synthetic HMW-glutenin gene and future modifications are intended to a

34 ive receptor kinase gene near the y-type HMW-glutenin gene at the Glu-B1 locus is likely active as it

35 uplicate globulin gene, found 5' of each HMW-glutenin gene, assists to tentatively define the origina

36 f six genes including the two paralogous HMW-glutenin genes are disrupted in the orthologous region o

37 -type ( Glu-1-1 ) and y-type ( Glu-1-2 ) HMW-glutenin genes of the complex Glu-B1 locus were found to

38 s one of the two high-molecular-weight (HMW) glutenin genes, comprising the complex Glu-B1 locus.

39 leading to the paralogous x- and y-type HMW-glutenin genes.

40 ion in terms of protein fractions (gliadins, glutenins) has been determined by means of RP-HPLC, to a

41 lacking IgE to omega(5) -gliadin, and to HMW glutenin in 59%.

42 xhibited the known anomalous behavior of HMW-glutenins in SDS-PAGE.

43 equences may be attributed to more polymeric glutenin incorporated in the network through thiol (SH)/

44 nd height; the ratio of insoluble to soluble glutenin is influential factor and this ratio should be

45 ression of gliadins and low-molecular-weight glutenins (LMWgs) by active demethylation of their promo

46 tinct types of allelic variations at the HMW-glutenin loci in the A genomes of different hexaploid wh

47 tig covering the high molecular weight (HMW)-glutenin locus from the A genome of durum wheat (Triticu

48 macropolymers, larger size distribution for glutenin macropolymer particles and varied sodium-dodecy

49 an lower MW PA, whereas both PA precipitated glutenins more efficiently than gliadins.

50 e that too much gliadin incorporation in the glutenin network during pasta processing tightens the pr

51 ndary structure, and extractable gliadin and glutenin of gluten were analyzed to elucidate gluten str

52 Most likely, KIO3 caused glutenin oxidation within each individual dough layer to

53 gated into five domains: peak I (130-30 kDa; glutenins), peak II (55-20 kDa; gliadins), peak III (28-

54 arinograph, respectively, while gliadins and glutenins profiling was done by SDS-PAGE.

55 -1 locus, encoding the high-molecular-weight glutenin protein subunits, controls bread-making quality

56 The gene expressed the novel HMW-glutenin protein to relatively high levels in bacterial

57 cus, on wheat albumin, globulin, gliadin and glutenin proteins during heat treatment of wheat dough a

58 ), gluten index (r=0.959( * *)), and gliadin/glutenin ratio (r=-0.952( * *)), while peak II influence

59 tained 32 identical copies of one of the HMW-glutenin repetitive domain motifs.

60 tic dissection of the molecular basis of HMW-glutenin role in the visco-elastic properties critical f

61 Known gliadin and glutenin sequences were largely determined through cloni

62 These changes concerned mainly glutenins since beta-structures are characteristic for t

63 During pasta drying, glutenin starts polymerizing already below 60 degrees C

64 synthetic wheat high-molecular-weight (HMW) glutenin storage protein gene analog was constructed for

65 ive abundance of three high molecular weight glutenin sub units (HMW-GS) were decreased at e[CO2].

66 called T-A-1 from the high molecular weight glutenin subunit (HMW-GS) Dx5 were measured to obtain ne

67 ted comprising a wheat high molecular weight glutenin subunit gene promoter, a 304-bp sucrose non-fer

68 High molecular weight glutenin subunit genes explained much of the heritable v

69 substantial amounts of high-molecular-weight glutenin subunits (HMW-GS) from wheat.

70 of the protein fractions available: high MW glutenin subunits (HMW-GS) over low MW-GS, and omega-gli

71 High-molecular-weight glutenin subunits (HMW-GS), one class of seed storage pr

72 up of gluten proteins, high molecular weight glutenin subunits (HMW-GS), plays an important role in d

73 perm, particularly the high-molecular-weight glutenin subunits (HMW-GS), which are important in deter

74 , glutenin and purified low molecular weight glutenin subunits (LMW-GS) using a 4 g sample Microdough

75 The varieties that possesses high MW glutenin subunits combinations of 91 kDa + 84 kDa + 78 k

76 for portions of high molecular weight (HMW) glutenin subunits were identified by sequence analysis o

77 quence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of ce

78 es against gliadin and high-molecular-weight glutenin subunits.

79 d in omega-gliadins and low-molecular-weight glutenins that had been identified as specific targets o

80 Gliadins and glutenins, the major storage proteins of wheat endosperm

81 hen the pointer changes towards to insoluble glutenin; the dough is more resistant, the bread is more

82 ents were registered in the phase diagram of glutenins up to 80 degrees C, followed by partial refold

83 -gliadin, and high- and low-molecular-weight glutenin were commercially synthesized and coupled to Lu

84 The gliadins and glutenins were also reduced in vivo during germination--

85 a linear and quadratic fashion; extractable glutenins were not affected.

86 n 3A and 3C, chitinase, beta-amylase and LMW glutenins, were identified from the electrophoretic patt

87 of the environmental triggers (gliadins and glutenins) with these gene products to trigger the immun