Asian Journal of Agricultural Sciences 3(6): 506-515, 2011
ISSN: 2041-3890
© Maxwell Scientific Organization, 2011
Submitted: August 30, 2011
Accepted: October 07, 2011
Published: November 15, 2011
Genetic Variability in Some Syrian Wheat Genotypes using Storage Proteins
¹Lina Mammdouh Alnaddaf, ²Mohammad Yahia Moualla and ³Abdul Rahman Kalhout
1
Field Crops Department, Faculty of Agriculture, Tishreen University, Lattakia, Syria
2
Field Crops Department, Faculty of Agriculture, Tishreen University, Lattakia, Syria
3
Biotechnology Department, GCSAR- Sci. Agricultural Research Center, Aleppo Syria
Abstract: Seed storage proteins (Glutenin & Gliadin) were used as an effective markers to assess genetic
diversity among 24 wheat genotypes((14) durum wheats and (10) bread wheats) using A-PAGE and SDSPAGE and determine the genotypes that had bands which used as marker to good quality . In durm wheats,
Jorjet, kechek , sham9 and kahlahadba recognised by gamma 45 and subunits (17+18) that had positive effect
on the dough. In bread wheats, Abozec, Sham10, Doma32058, Doma32457, Doma4, Bohoth8 have good
technology characteristics due to that have subunits (5+10). The results obtained in this study are useful in
breeding programs to improve quality by selecting of the best genotypes.
Key words: A-PAGE, electrophoresis, genetic variability, gliadin, glutenin, SDS-PAGE, storage proteins,
wheat
INTRODUCTION
Wheat is one of the most important food crops of the
world, feeding about 40% (nearly half) of the world
population and providing 20% (one fifth) of total food
calories and protein in human nutrition (Gupta et al.,
2008). Two types of wheat are cultivated in syria:
Triticum aestivum (bread wheat), Triticum durum (durum
wheat). The total production was 2.139 m tones and The
yield was 1440 Kg/H in 2008 (FAO, 2008).
Gluten proteins, that comprise gliadin and glutenin,
represent about 80% of total protein in the wheat grain
and are considered to contribute to the viscosity and
extensibility (gliadin), and elasticity (glutenin) of the
gluten mass (Bietz and Wall, 1973; Pomeranz, 1988). The
gliadins constitute about 40% of the total endosperm
protein. Shewry et al. (1986) defined gliadins as
monomeric proteins with intramolecular disulphide bonds,
and that the conformations are thus stabilised by hydrogen
bonds and hydrophobic interactions (Kasarda et al.,
1984). When fractioned by A-PAGE (acid polyacrylamide
gel electrophoresis) they are subgrouped into ", $, ( and
T gliadins (Radiƒ et al., 1998).
Gliadins are encoded by six Gli loci mapped to the
short arms of homoeologous group 1(Gli-A1, Gli-B1 and
Gli-D1) and 6 (Gli-A2, Gli-B2 and Gli-D2) chromosomes
(Wrigley and Shepard, 1973; Harsch et al., 1997). There
is considerable variation in gliadin-banding patterns
between varieties, making it possible to use A-PAGE to
identify varieties (Wrigley, 1992). Glutenins are
polymeric proteins stabilized by disulfide bonds (Kasarda,
1989; Mac-Ritchie and Lafiandra, 1997) that, when
treated with a reducing agent, release high molecular
weight glutenin subunits (HMW-GS; 90 to 140 KDa) and
low molecular weight glutenin subunits (LMW-GS; 30 to
75 KDa) (Gianibelli et al., 2001; Payne et al.,1984). The
HMW-GS are encoded by genes at three loci, Glu-A1,
Glu-B1 and Glu-D1, located on the long arms of
homoeologous group1 chromosomes (Payne et al., 1981;
Payne and Lawrence, 1983). Molecular studies have
shown that each locus contains two tightly linked genes
which encode two types of HMW-GS one of higher
molecular weight, designated the x-type, and the other of
lower molecular weight designated the y-type (Harberd
et al., 1986; Payne et al., 1981; Shwery et al., 1992).
Alleles coding for different subunits occur at all three loci
(Lawrence and Shepherd, 1981; Payne et al., 1981) and
are manifested as one or more subunit combinations,
resulting in a high degree of subunit polymorphism in
both bread and durum wheat cultivars (Payne and
Lawrence, 1983; Branlard et al., 1989). The
polymorphisms of glutenin coding alleles have been well
described (Payne and Lawrence, 1983; Payne, 1987;
Rogers et al., 1989; Gupta and Shepherd, 1990; Carrillo
et al., 1990; Metakovsky, 1991) and these are known to
account for a part of the range in bread-making ability and
pasta quality, depending on the fraction involved (Gupta
et al., 1989; Khelifi and Branlard, 1992). Glutenin
proteins are responsible in part for the quality differences
between durum and bread wheat (Vazquez et al., 1996;
Rao, 2008) and the extensive variation at the Glu-1 loci
could be exploited as a complementary marker for
pedigree analysis and variety identification (Bahraei et al.,
2004).
Intensive plant breeding during the past century has
narrowed the genetic base of wheat by replacing wheat
Corresponding Author: Lina Mammdouh Alnaddaf, Assistant in Field Crop Department -Faculty of Agriculture,
Tishreen University-Lattakia-Syria
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Asian J. Agric. Sci., 3(6): 506-515, 2011
Table 1: Gliadin analysis of wheat varieties
GLI1
GLI2
Abozec
1
1
Joda 2
0
0
Shahba
0
0
Joda 3
0
0
Sham 6
1
1
Sham 10
1
1
Doma 32058 1
1
Doma 32486 1
1
Doma 32457 1
1
Doma 32466 1
1
Doma 4
1
1
Bohoth 8
1
1
Doma 17322 1
1
Kchek
0
0
Jorjet
0
0
Doma 29868 0
0
Sham 7
0
0
Bohoth 9
0
0
Bohoth 11
0
0
Doma 1
0
0
Sham 9
0
0
Doma 3
0
0
Akbach
0
0
Khlahadba
0
0
GLI8
GLI9
Abozec
0
0
Joda 2
1
1
Shahba
1
0
Joda 3
0
1
Sham 6
1
0
Sham 10
1
1
Doma 32058 1
1
Doma 32486 1
1
Doma 32457 1
1
Doma 32466 1
1
Doma 4
1
0
Bohoth 8
1
0
Doma 17322 1
0
Kchek
1
0
Jorjet
1
0
Doma 29868 1
0
Sham 7
1
0
Bohoth 9
1
0
Bohoth 11
1
0
Doma 1
1
0
Sham 9
1
0
Doma 3
1
0
Akbach
1
1
Khlahadba
1
0
GLI3
0
0
0
0
0
0
0
0
0
0
0
0
0
1
1
1
1
1
1
1
1
1
0
1
GLI10
0
0
0
0
0
1
1
1
1
1
0
1
1
0
0
0
0
0
0
0
0
0
1
0
GLI4
0
0
1
0
0
0
0
0
0
0
1
0
0
0
0
0
0
0
0
0
0
0
0
1
GLI11
0
1
1
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
C
landraces with modern wheat cultivars and that this could
limit future crop improvement and could be consider as an
example of genetic Drift caused by man (Khan, 2003;
Sultana et al., 2007; Zeb et al., 2007; Tahir et al., 1995)
Therefor we can used Wheat storage proteins in:
C
C
C
C
C
Used for cultivar identification in hexaploid and
tetraploid wheats (Mir Ali et al., 1999b).
Evaluate the biochemical characterization of wheat
genotypes (Redaelli et al., 1997; Payne et al., 1981;
Solouki and Abbasali, 2007; Shuaib et al., 2007;
Kissimon et al., 2003; Mir Ali, 1999 a, b).
Support and develop wheat breeding programs
(Pflüger et al., 1994; Ram et al., 2005).
GLI5
0
0
0
0
0
0
0
0
0
0
0
1
1
1
1
1
1
1
1
1
1
1
0
0
GLI12
1
0
0
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
0
1
GLI6
0
0
1
0
0
1
1
1
1
1
0
0
0
0
0
0
0
0
0
0
0
0
0
0
GLI13
0
0
0
0
0
0
0
1
0
0
0
0
1
1
1
1
1
1
1
1
1
1
0
1
GLI7
1
1
1
0
1
1
1
1
1
1
0
1
1
1
0
0
0
0
0
0
0
0
0
1
Determine whether heterogeneity is due to genetic or
mechanical admixing (Mir Ali et al., 2000).
Identification of novel types of HMW-GS with
unusual structures and properties (Gobaa et al., 2007;
Liu et al., 2007; Yan et al., 2009).
Determining dough properties and bread making
quality (Gianibelli et al., 2001; MacRitchie and
Lafiandra, 2001; Blechl et al., 2004; Gupta and
MacRitchie, 1994; Kasarda, 1989; Shwery et al.,
1992).
In the present study, we have determined the gliadin
and HMW glutenin subunits composition for some Syrian
wheat genotypes. The objectives were:
507
Asian J. Agric. Sci., 3(6): 506-515, 2011
Table 2: HMW – glutenin analysis of wheat varieties
GLU1
GLU2
GLU3
Abozec
0
0
1
Joda 2
0
0
0
Shahba
0
0
0
Joda 3
0
0
0
Sham 6
0
0
0
Sham 10
0
0
0
Doma 32058 0
0
0
Doma 32486 0
0
0
Doma 32457 0
0
0
Doma 32466 0
0
0
Doma 4
0
0
0
Bohoth 8
0
0
0
Doma 17322 0
0
0
Kchek
0
0
0
Jorjet
0
0
0
Doma 29868 0
1
0
Sham 7
0
0
0
Bohoth 9
0
0
0
Bohoth 11
0
0
0
Doma 1
0
0
0
Sham 9
0
0
0
Doma 3
0
0
0
Akbach
0
0
0
Khlahadba
0
0
0
GL8
GLU9
GLU10
Abozec
0
0
0
Joda 2
0
0
0
Shahba
0
1
0
Joda 3
0
0
0
Sham 6
0
0
0
Sham 10
0
0
0
Doma 32058 0
0
0
Doma 32486 0
0
0
Doma 32457 0
0
0
Doma 32466 0
0
0
Doma 4
0
0
0
Bohoth 8
0
0
0
Doma 17322 0
0
0
Kchek
0
0
0
Jorjet
0
0
0
Doma 29868 0
1
0
Sham 7
0
0
0
Bohoth 9
1
0
0
Bohoth 11
1
0
0
Doma 1
0
1
0
Sham 9
0
0
0
Doma 3
0
1
1
Akbach
0
0
1
Khlahadba
0
0
0
C
C
GLU4
0
0
0
0
1
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
0
GLU11
0
1
1
0
1
1
1
1
1
1
1
1
1
0
0
0
1
0
0
0
1
0
0
0
Studying of Genetic variation for some Syrian wheat
genotypes by using A-PAGE (acid polyacrylamide
gel electrophoresis), SDS-PAGE (Sodium Dodecyl
Sulphate Polyacrylamide Gel Electrophoresis)
Determine the genotypes that had bands which used
as marker to good quality
GLU5
0
0
0
0
0
0
0
1
0
1
0
0
0
0
0
0
0
0
0
0
0
0
0
0
GLU12
0
0
0
0
0
0
0
0
0
0
0
0
0
1
1
0
0
0
0
0
0
0
0
0
GLU6
0
0
0
0
0
1
1
0
1
0
1
1
1
0
0
0
0
0
0
0
0
0
0
0
GLU13
1
0
1
1
0
0
0
1
0
0
0
0
0
0
0
1
0
0
0
0
0
0
0
0
GLU7
0
0
0
0
0
1
1
0
1
0
1
1
0
0
0
0
0
0
0
0
0
0
0
0
GLU14
0
1
0
0
0
0
0
0
0
0
0
0
0
0
0
0
1
1
1
1
0
0
0
0
Durum genotype: Kchek, Jorjet, Joda2, Joda3, Akbach,
Kahlahadba, Shahba (landraces). Sham7, Bohoth11,
sham9, Doma3, Doma1, Bohoth9, Doma 29868 (modern).
Bread genotypes: Abozec, Doma32457, Doma32466,
Sham6, Sham10, Doma4, Doma32058, Bohoth8,
Doma32486, Doma17322 (modern).
MATERIAL AND METHODS
Analytical methods: Two electrophoretic systems were
utilized A-PAGE of Bushuk and Zillman (1978) for
gliadin separation and the SDS-PAGE of laemmli (1970)
as modified by Payne et al. (1981) for HMW glutenin
separation. About 50 mg of crushed grains were used
Plant material: Twenty four varieties were obtained from
the General Commission For Scientific Agricultural
Research, they included (14) genotypes of durum wheat
and (10) genotypes of bread wheat.
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Asian J. Agric. Sci., 3(6): 506-515, 2011
Table 3: HMW-GS and quality scores in durum genotypes
HMW-GS at Glu-1
---------------------------------------------Durum Genotypes
Glu-A1
Glu-B1
Glu-D1
Kchek
Null
17+18
Jorjet
Null
17+18
Doma29868
2*
20
Sham7
Null
7+8
Bohoth 9
Null
6+8
Bohoth 11
Null
6+8
Doma1
Null
7+8
Sham 9
Null
17+18
Doma 3
Null
7+8
Akbach
2*
17+18
Kahlahadba
Null
17+18
Joda2
Null
7+8
Shahba
Null
7,17+18
Joda3
Null
6+8
-
Quality scores
-------------------------------------------Glu-A1
Glu-B1
Glu-D1
1
3
1
3
3
1
1
3
1
1
1
1
1
3
1
3
1
3
3
3
1
3
1
3
1
1
1
-
Total
4
4
4
4
2
2
4
4
4
6
4
4
2
Table 4: HMW-GS and quality scores in bread genotypes
HMW-GS at Glu-1
---------------------------------------------Bread genotypes
Glu-A1
Glu-B1
Glu-D1
Abozec
Null
17+18
5+10
Sham6
Null
7
2+12
Sham 10
2*
7
5+10
Doma32058
2*
7
5+10
Doma 32486
Null
7
2+12
Doma 32457
2*
7
5+10
Doma 32466
2*
7
2+12
Doma 4
2*
7
5+10
Bohoth8
2*
7
5+10
Doma 17322
2*
7+8
2+12
Quality scores
-------------------------------------------Glu-A1
Glu-B1
Glu-D1
1
3
4
1
1
2
3
1
4
3
1
4
1
1
2
3
1
4
3
1
2
3
1
4
3
1
4
3
3
2
Total
8
4
8
8
4
8
6
8
8
8
from each genotype. Analysis were performed in the
Laboratory of Biotechnology- Biotechnology DepartmentGCSAR- Sci. Agri. Res. Center-Aleppo-Syria in 2010.
slab gel electrophoresis unit. A constant current of 25 mA
was used to run two gels for 16 h.
Data analysis: Allelic forms of the three loci were
identified following the designation of Payne and
Lawrence (1983). Bands, presence (1) and absence (0),
were recorded for all genotypes (Table 1, 2). Data were
combined together to calculate the genetic similarities
between studied individuals using Dice coefficient (GS(ij)
= 2a/(2a+b+c) Dice (1945), followed by setting up the
cluster analysis by (UPGMA) Unweighted Pair Group
Mean Arithmetic Average method (Fig. 5). Quality
scores were assigned to individual or subunit pairs based
on Payne (1987) (Table 3, 4).
A-PAGE: The gliadins were extracted by adding 165
70% ethanol, vortexed and mixed for 2.30 h then
centrifuged for 15 min at 15000 rpm in an Eppendorf
microcentrifuge.100 from the supernatant were added to
85 of 60% (v/v) glycerin and a 40 of the mixture was run
on 6% Acrylamide gels (200.220.1mm) using an electric
current of 40 mA for 4 h. Each gel contained 12
genotypes in addition to the Canadian variety Marquis as
a control. The middle dense band of Marquis was given a
Relative Mobility (RM) of 50 (Bushuk and Zillman,
1978) and the RM of all bands in each gel were computed
accordingly.
RESULTS
SDS-PAGE: The HMW glutenins were extracted from
the residue of the same samples and fractionated in 10%
w/v polyacrylamide gels. Each sample was suspended in
a medium containing 2%(w/v) SDS, 5%(w/v) 2mercaptoethanol, 0.001%(w/v) pyronin,10%(v/v) glycerol
and 0.063M Tris-HCl (pH 6.8). The samples were left for
90 minutes at room temperature and shaken every 15
minutes. Later, they were placed in a boiling water bath
for 1.30 min and allowed to cool and were put in an
Eppendorf microcentrifuge for 15 min at 15000 rpm.15
from each sample were placed into each slot of a vertical
A-PAGE variability: A-PAGE allowed gliadin
separation into four groups depending on their relative
mobility(RM): T-gliadins which migrate up to( RM = 39),
(-gliadins (RM = 40-56), $-gliadins (RM = 57-68) and "gliadins (RM = 69-80).Varieties differed in the number of
bands and this ranged between 2 and 6 for durum wheats
(Fig. 1) and between 4 and 9 for bread wheats(Fig. 3).
Durum wheats were distinguished by having the first band
appearing at RM =18.6, whereas bread wheat varieties
had their first band at RM = 13.2. The genotypes of
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Asian J. Agric. Sci., 3(6): 506-515, 2011
Fig. 1: A-PAGE separation of gliadin in durum genotypes. M: Marquis; 1: Kchek; 2: Jorjet; 3: Doma 29868; 4: Sham7; 5: Bohoth
9; 6: Bohoth11; 7: Doma1; 8: Sham 9; 9: Doma 3; 10: Akbach; 11: Kahlahadba
Fig. 2: SDS-PAGE separation of HMW-GS subunits in durum genotypes. M: Marquis; 1: Kchek; 2: Jorjet; 3: Doma 29868; 4:
Sham7; 5: Bohoth 9; 6: Bohoth11; 7: Doma1; 8: Sham 9; 9: Doma3; 10: Akbach; 11: Kahlahadba
Fig. 3: A-PAGE. separation of gliadin in bread genotypes. M: Marquis; 1:Abozec; (2: Joda2; 3: Shahba; 4: Joda3) Durum Wheat;
5: Sham6; 6: Sham 10; 7: Doma 32058; 8: Doma 32486; 9: Doma 32457; 10:Doma 32466; 11: Doma 4; 12: Bohoth 8;
13:Doma 17322
510
Asian J. Agric. Sci., 3(6): 506-515, 2011
Fig. 4: SDS-PAGE separation of HMW-GS subunits in bread genotypes. M: Marquis;1:Abozec;(2: Joda2; 3: Shahba; 4: Joda3)
Durum Wheat; 5: Sham6; 6: Sham 10; 7: Doma 32058; 8: Doma 32486; 9: Doma 32457; 10:Doma 32466; 11: Doma 4; 12:
Bohoth 8; 13:Doma 17322
Fig. 5: Dendrogram of 24 wheat varietyes based on Dice similarity coefficient and (UPGMA) .*: Acsad1229 = Doma3; Doma41004:
sham9; Acsad901: Doma4; Doma19918: Bohoth8
Drum wheats which had (-Gliadin (45) band were Kchek,
Jorjet, Doma29868, Sham7, Bohoth9, Bohoth11, Doma1,
sham9, Doma3 and Kahlahadba (Fig. 1).
Akbach) carried 2* subunit .The highest frequency in the
total number of tested genotypes was that of subunits
17+18 followed by subunits 7+8, 6+8 and lastly subunit
20 and subunit 7. In bread wheat (Fig. 4,Table 4): Two
subunits (2*, Null) were recognized at Glu-A1, three (7,
7+8, 17+18) at Glu-B1 and two (5+10, 2+12) at Glu-D1
locus.
SDS-PAGE variability: The number of HMW-GS
present in most durum wheat genotypes were 2-3 whereas
4-5 in bread wheat genotypes. In durum wheat
(Fig. 2, Table 3): All genotypes under study had the null
allele in Glu-A1locus except two genotypes (Doma29868,
DISCUSSION
511
Asian J. Agric. Sci., 3(6): 506-515, 2011
Genetic diversity is the basis for successful crop
improvement and can be estimated by different methods
(Fufa et al., 2005). Seed storage proteins are used to study
genetic variability in durum and bread wheats by using APAGE (Gliadin), SDS-PAGE (Glutenin). The application
of protein electrophoresis of gliadins using A-PAGE has
long been used for variety fingerprinting (Bean and
LookHart, 2000) due to the higher complexity in the
number of genes and also in the multiplicity of the allelic
variation (Metakovsky and Branlnd, 1998) resulting in
much higher amount of bands compared to SDS-PAGE.
Gliadins have been reported to be more complex in their
genetic structure than glutenin. Pogna et al. (1993)
reported a presence of 3-10 active genes in each of the
Gli-1 loci, and each of these genes has been estimated to
have a number of alleles that varies between 12-30.
Metakovsky et al. (1997) proposed that the differences
among wheat varieties are due to the presence of different
allelic combinations in each variety. The distinction
between durum and bread wheat varieties in protein
electrophoresis studies has been realized and attributed to
the absence of D genome in durum wheat. Durum wheats
have a different electrophoretic pattern to that of bread
wheat. No durum wheat genotypes carried bands with
RM<15. The results of this study showed that T gliadin
was characterized by a large number of bands (1-5) in
durum wheat, and (3-7) bands in bread wheat. (Joda3)
contained one protein band in the T-gliadin, while
(shahba) had the largest number of protein bands with (5).
Bread wheat (Abozec) had less number of bands in the w
region (3), followed by (Sham6, Doma 4) that had four
bands in the same area. Wellner et al. (1996) reported that
it is due to the lack of sulfur in T gliadins that this group
is affected by hydration. Also, Fido et al. (1997) found
this gliadin group had the most negative effect on dough
strength followed by ", $, with ( gliadins having the least
negative effect. In addition, Mir Ali (2000) found that the
hourani variety (known to have superior quality) carried
only two T gliadin bands. Our results indicated that there
was 10 genotypes which had g-45. In the last twenty years
many scientists and researchers have focused their studies
on the seed storage proteins due to the increasing
evidences of their impact on technological properties both
in durum and bread wheat. A high protein content,
however, does not always assure the good quality of
pasta. It has been ascertained that specific protein
components of seed storage prolamin proteins are
correlated with the technological properties of durum
wheat flour (Carrillo et al., 1999). Early studies
(Damidaux et al., 1978; Kosmolak et al., 1980; Du Cros
et al., 1982) demonstrated the usefulness of two (
gliadins: g-45 and g-42 (encoded at the Gli-B1 locus) as
markers of good and poor pasta quality, respectively. In
durum wheats Results showed most of genotypes
contained null allele in Glu-A1 which had a negative
effect on quality traits compared with 2* subunit at the
same locus that had an identical impact on the strength
and extensibility of the dough (Branlard et al., 2001). At
Glu-B1, the best alleles were 17+18 and 7+8 due to a
positive correlation between these subunits and dough
quality. Numerous studies reported that subunits 17+18
had a positive effect on dough than subunit 20 (20x+20y)
(Gianibelli et al., 2001). These differences in dough
strength were due to differences in molecular size of
glutenin polymers deduced from solubility measurements
(Gupta and Mac-Ritchie 1994).
The HMW glutenin subunit genes on chromosome
1A appear to have a negligible relationship to durum
quality parameters when compared to genes on
chromosome 1B (Pogna et al., 1990). In bread wheats
among seven allelic variants detected in this study subunit
2* at Glu-A1 was the most frequent in genotypes. The
most frequent subunits at the Glu-B1 were 7, 17+18, 7+8.
At Glu-D1 locus two pairs of subunits 5+10, 2+12 were
present in genotypes. The most important locus that
distinguishes bread wheat is Glu-D1. Redaelli et al.
(1997) established that allelic variation at the Glu-D1
locus had a greater influence on bread-making quality
than the variation at the Glu-A1 and Glu-B1 loci. In bread
wheat, the HMW-GS 1Dx5 + 1Dy10 encoded by the GluD1d locus are associated with good bread-making quality
and increased dough strength, while 1Dx2 + 1Dy12
encoded by Glu-D1a are associated with poor breadmaking quality and weak dough (Payne et al., 1984;
Payne, 1987; Shwery et al., 1992; Gianibelli et al., 2001).
The superior quality of the Glu-D1d allele is generally
attributed to the difference in amino acid primary
structures of 1Dx2 and 1Dx5. According to Shewry and
Tatham (1997), 1Dx5 has one additional cysteine residue
and therefore can form longer polymer chains, resulting
in higher elasticity of the dough. Glu-1 quality scores for
each genotype according to Payne (1987) are showen in
(Table 3, 4). The average score of the bread wheats
analysed was (7) and showed that the HMW-GS
compositions were of generally good quality (Table 4). In
durum wheats, Akbach genotype had a high quality scores
based on HMW-GS (Table 3). The dendrogram calculated
from Dice similarity coefficient and (UPGMA)
Unweighted Pair Group Mean Arithmetic Average
method. The results showed (Fig. 5) that the value of
average genetic similarity between bread and durum
wheat was 45%.The dendrogram resulted showed two
separate clusters according to the genome level the
tetraploid level (durum wheat) and the hexaploid level
(bread wheat). In addition, the presence of landraces
genotypes with modern varieties and this is due to genetic
512
Asian J. Agric. Sci., 3(6): 506-515, 2011
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relationship resulting from crosses between them, add to
that the fact that the modern varieties originated from
landraces genotypes. The bootstrap values for this
dendrogram ranges from 8 to100%. Tavale (2001)
considered that the genotype with bootstrap values below
50% indicate that the positions of these genotypes may
change if other marker systems are applied or other
genotypes are involved in the analysis. This information
could be used by wheat breeders to select appropriate
sources of specific genes related with end-product quality.
CONCLUSION
From the result of this study it is concluded that the
electrophoresis of seed Storage proteins used for variety
fingerprinting and that methods are reliable, simple,
repeatable and economic procedure and can be utilized by
wheat breeders to detect variability among wheat
genotypes to identify new sources of variation that could
be used in crop improvement programs.
ACKNOWLEDGMENT
We thank Dr. Suha Abdul Raouf ashtarBiotechnology Department-GCSAR- Sci. Agri. Res.
Center-Aleppo –Syria.
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