A RELATIONSHIP BETWEEN DURUM WHEAT QUALITY AND GLIADIN ELECTROPHOREGRAMS

1980 ◽  
Vol 60 (2) ◽  
pp. 427-432 ◽  
Author(s):  
F. G. KOSMOLAK ◽  
D. LEISLE ◽  
J. E. DEXTER ◽  
R. R. MATSUO ◽  
B. A. MARCHYLO
Keyword(s):  
Durum Wheat ◽  
Gel Electrophoresis ◽  
Cooking Quality ◽  
Triticum Turgidum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Quality Characteristics ◽  
Polyacrylamide Gel ◽  
Wheat Quality ◽  
Group I ◽  
Group Ii

Gliadins from 30 durum wheat (Triticum turgidum L.) cultivars grown at three locations were extracted and separated by polyacrylamide gel electrophoresis. Cultivars could be classified as belonging to one of two groups based on the presence or absence of two bands (designated 42 and 45 according to their mobility) in their electrophoregrams. The two groups were compared for quality characteristics. Cultivars in group I (band 42 present, 45 absent) were characterized by weak gluten properties and poor cooking quality compared to the cultivars in group II (band 45 present). The results corroborate previous reports by other workers that a relationship exists between gliadin composition and durum wheat quality.

ASSOCIATION OF GLUME COLOR WITH GLUTEN STRENGTH AND GLIADIN PROTEINS IN DURUM WHEAT

1981 ◽  
Vol 61 (1) ◽  
pp. 149-151 ◽  
Author(s):  
D. LEISLE ◽  
F. G. KOSMOLAK ◽  
M. KOVACS
Keyword(s):  
Durum Wheat ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Triticum Turgidum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Gluten Strength

Lines of durum wheat (Triticum turgidum L.) were studied for glume color, gluten strength as determined by micromixograph and sodium-dodecyl-sulphate (SDS) sedimentation methods, and banding of gliadin proteins by polyacrylamide gel electrophoresis. The results indicated a linkage of factors controlling glume color and gliadin proteins. There also appeared to be an association of these two characteristics with gluten strength.

scholarly journals Similarity of cultivars of wheat (Triticum durum) on the basis of composition of Gliadin alleles

Genetika ◽  
2011 ◽  
Vol 43 (3) ◽  
pp. 527-536
Author(s):  
Nevena Djukic ◽  
Desimir Knezevic ◽  
Daniela Horvat ◽  
Dragan Zivancev ◽  
Aleksandra Torbica
Keyword(s):  
Durum Wheat ◽  
Gel Electrophoresis ◽  
Triticum Durum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Wheat Cultivars ◽  
Allele Composition ◽  
Gliadin Alleles

Twenty one durum wheat cultivars originating from different world countries were investigated. Composition of gliadins was analyzed by acid polyacrylamide gel electrophoresis. Allele composition of gliadins was determined on the basis of identified gliadin blocks. Polymorphisms of Gli- loci was established and 27 different gliadin alleles were identified, namely, 5 at Gli-A1, 4 at Gli-B1, 9 at Gli-A2 and 9 alleles at Gli-B2 locus. The catalogue of determined alleles was presented. Frequency of alleles ranged from 4.76% to 42.86%. Heterozygous Gli-loci were identified at two durum cultivars. Similarity among cultivars was studied on composition of Gli-alleles and presented by UPGMA dendogram. On the base of Gli-allele composition, similarity varied from 0% to 100%.

scholarly journals Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

1986 ◽  
Vol 234 (2) ◽  
pp. 305-310 ◽  
Author(s):  
G P Cottam ◽  
D M Moran ◽  
R Standring
Keyword(s):  
Amino Acid ◽  
Lolium Perenne ◽  
Grass Pollen ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Published Data ◽  
Pollen Extract ◽  
Rye Grass ◽  
Group I

Three fractions of rye-grass (Lolium perenne) pollen extract have been isolated by preparative isoelectric focusing (i.e.f.) and characterized in terms of physicochemical and immunochemical properties. The purified components were designated ‘R7’ and ‘R14’ on the basis of their positions in relation to other rye-grass pollen extract components on SDS/polyacrylamide-gel electrophoresis and their apparent molecular masses were assessed as 31 and 11 kDa respectively. On i.e.f., R14 split into two components, one acidic (pI 5.0) and one basic (pI 9.0), termed ‘R14a’ and ‘R14b’ respectively, and R7 focused at pI 5.8. R7 and R14a were shown to be allergenic by skin-prick test and all three components were recognized by rye-grass-pollen-specific human IgE. On SDS/polyacrylamide-gel electrophoresis and i.e.f., R7 behaved in a manner identical with that shown by an authentic sample of Rye I and gave an amino acid analysis similar to published data [Johnson & Marsh (1966) Immunochemistry 3, 91-100] for Rye group-I isoallergens; the amino acid sequence of the first 27 N-terminal amino acids was also determined. Physicochemical analysis revealed that R14a was equivalent to Rye II and 14b to Rye III. Preparative i.e.f. followed by gel-permeation chromatography proved to be a rapid and efficient method for purifying the allergenic components of Rye I (R7), Rye II (R14a) and Rye III (R14b) from rye-grass pollen extract.

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak
Keyword(s):  
Gel Electrophoresis ◽  
Functional Relationship ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Functional Similarity ◽  
Fractionation Method ◽  
Relationship Of ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule ◽  
Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

2018 ◽  
Vol 26 (2) ◽  
pp. 058
Author(s):  
Anna P. Roswiem ◽  
Triayu Septiani
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page

<em>Bahan<strong> </strong>baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE).<strong> </strong>Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi  dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.</em>

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