Erratum: Gliadin alleles in Canadian western red spring wheat cultivars: use of two different procedures of acid polyacrylamide gel electrophoresis for gliadin separation

Genome ◽  
1994 ◽  
Vol 37 (2) ◽  
pp. 349-349
Author(s):  
E. V. Metakovsky ◽  
P. K. W. Ng ◽  
V. M. Chernakov ◽  
N. E. Pogna ◽  
W. Bushuk
Keyword(s):  
Spring Wheat ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Wheat Cultivars ◽  
Gliadin Alleles

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%.

Gliadin alleles in Canadian western red spring wheat cultivars: use of two different procedures of acid polyacrylamide gel electrophoresis for gliadin separation

Genome ◽  
1993 ◽  
Vol 36 (4) ◽  
pp. 743-749 ◽  
Author(s):  
E. V. Metakovsky ◽  
P. K. W. Ng ◽  
V. M. Chernakov ◽  
N. E. Pogna ◽  
W. Bushuk
Keyword(s):  
Common Wheat ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Component Composition ◽  
Polyacrylamide Gel ◽  
Marker Genes ◽  
Wheat Cultivars ◽  
Gliadin Alleles ◽  
Gliadin Allele ◽  
Spring Common Wheat

Gliadin allele compositions of 21 Canadian spring common wheat cultivars, most of which belong to the Canada western red spring (CWRS) class, were studied and great similarity in their genotypes was confirmed. It was found that alleles frequent in the set of Canadian wheats (such as Gli-B1d, Gli-D1j, Gli-A2m, and Gli-D2h) are very rare or absent in common wheat cultivars from other regions and countries studied earlier, indicating that germplasm of CWRS cultivars is rather unique. It may be suggested that alleles frequent in Canadian cultivars relate to important technological characteristics of these wheats and may possibly serve as marker genes during selection for quality traits. Similarity of gliadin electrophoregrams obtained by two different acid polyacryl-amide gel electrophoretic procedures for the same genotype was established, and the component composition of allelic variants of blocks of gliadin components found in the set of Canadian cultivars and in standard cultivars Chinese Spring and Bezostaya 1 are described.Key words: gliadin alleles, acid polyacrylamide gel electrophoresis, Canadian bread wheats.

scholarly journals Polymorphism of Gli-D1 alleles of Kragujevac’s winter wheat cultivars (Triticum aestivum L.)

Genetika ◽  
2007 ◽  
Vol 39 (2) ◽  
pp. 273-282
Author(s):  
Desimir Knezevic ◽  
Aleksandra Novoselskaya-Dragovich
Keyword(s):  
Triticum Aestivum ◽  
Winter Wheat ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel ◽  
Wheat Cultivars ◽  
Number Of Components ◽  
Winter Wheat Cultivars

Composition of gliadins encoded by Gli-D1 allele as well polymorphisms of Gli-D1 allele investigated in 25 wheat cultivars by using acid polyacrylamide gel electrophoresis. Electrophoregrams obtained by polyacrylamide gel electrophoresis were used for estimation variability of gliadin components and identification of gliadin blocks. Five gliadin blocks encoded by different alleles at Gli-D1 locus were apparently expressed and identified. Gliadin blocks differed according to number of components and their molecular mass. Variability of determined block components indicates that existing polymorphisms of gliadins alleles. Frequency of identified 5 alleles at Gli-D1 locus was in ratio from 4% to 52%. The highest frequency of b allele and the of g allele was found.

GLIADIN COMPOSITION OF THE BREAD-WHEAT CULTIVARS BW 20 AND SINTON

1979 ◽  
Vol 59 (4) ◽  
pp. 1001-1005 ◽  
Author(s):  
F. G. KOSMOLAK
Keyword(s):  
Bread Wheat ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Test Plot ◽  
Wheat Cultivars ◽  
Electrophoretic Patterns ◽  
Yield Test

Gliadins from 123 breeder lines of the cultivar BW 20 and from 198 breeder lines of the cultivar Sinton were extracted and separated by polyacrylamide gel electrophoresis. The cultivar BW 20 consisted of four biotypes and the cultivar Sinton of five with respect to their gliadin composition. The major biotype was represented by 93% of the breeder lines of the cultivar BW 20 and by 98% of the cultivar Sinton. The electrophoretic patterns of awned off-type plants in a yield test plot of Cultivar BW 20 were different from the patterns of the biotypes present in breeder lines of BW 20. It was concluded that these awned plants were contaminants from other cultivar sources.

WHEAT CULTIVAR IDENTIFICATION BY GLIADIN ELECTROPHOREGRAMS. I. APPARATUS, METHOD AND NOMENCLATURE

1978 ◽  
Vol 58 (2) ◽  
pp. 505-515 ◽  
Author(s):  
W. BUSHUK ◽  
R. R. ZILLMAN
Keyword(s):  
Electrophoretic Mobility ◽  
Spring Wheat ◽  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Wheat Cultivar ◽  
Polyacrylamide Gel Electrophoresis ◽  
Wheat Cultivars ◽  
Major Band ◽  
Hard Red Spring Wheat ◽  
Spring Wheat Cultivar

An apparatus and method are described for polyacrylamide gel electrophoresis of gliadins. Since the gliadin pattern (electrophoregram) is a genotypic character, electrophoresis offers a promising means for identifying wheat cultivars. Electrophoregrams are presented for a number of wheat cultivars to illustrate the results that can be obtained by the method described. A new nomenclature for gliadin bands (components) separated by this method is also presented. The nomenclature uses a major band in the electrophoregram of the Canadian hard red spring wheat cultivar Marquis as the reference. It was assigned an arbitrary mobility of 0.50; all other bands of Marquis and other cultivars are identified on the basis of electrophoretic mobility relative to 0.50 for the reference band under identical electrophoresis conditions.

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.

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