BARLEY CULTIVAR IDENTIFICATION BY ELECTROPHORETIC ANALYSIS OF HORDEIN PROTEINS: I. EXTRACTION AND SEPARATION OF HORDEIN PROTEINS AND ENVIRONMENTAL EFFECTS ON THE HORDEIN ELECTROPHOREGRAM

1980 ◽  
Vol 60 (4) ◽  
pp. 1343-1350 ◽  
Author(s):  
B. A. MARCHYLO ◽  
D. E. LaBERGE
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Analysis ◽  
Western Canada ◽  
Barley Cultivar ◽  
Barley Cultivars ◽  
Extraction And Separation ◽  
Acid Gel

Reproducible hordein electrophoregrams were obtained when hordeins, extracted from Canadian-grown barley cultivars, were subjected to polyacrylamide gel electrophoresis at acid pH (acid-gel PAGE). The hordeins were extracted at room temperature into a solution of 55% (vol/vol) isopropanol containing 2% (vol/vol) monothioglycerol. Extraction of hordein at high temperature (60 °C) produced significant reduction in the number of protein bands available for cultivar identification. Alkylation of the reduced hordeins, prior to acid-gel PAGE, did not improve the resolution or appearance of the hordein electrophoregrams. The effect of environment on the hordein electrophoregram was studied. Four barley cultivars were grown at eight locations in Western Canada during 2 successive years. Hordein electrophoregrams were qualitatively independent of growth location, year of growth and protein content. These results suggest that acid-gel PAGE should prove useful as a technique for barley cultivar identification.

BARLEY CULTIVAR IDENTIFICATION BY ELECTROPHORETIC ANALYSIS OF HORDEIN PROTEINS II. CATALOGUE OF ELECTROPHOREGRAM FORMULAE FOR CANADIAN-GROWN BARLEY CULTIVARS

1981 ◽  
Vol 61 (4) ◽  
pp. 859-870 ◽  
Author(s):  
B. A. MARCHYLO ◽  
D. E. LABERGE
Keyword(s):  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Analysis ◽  
Polyacrylamide Gel ◽  
Barley Cultivar ◽  
Relative Mobility ◽  
Malting Barley ◽  
Barley Cultivars ◽  
Acid Ph

Hordein proteins, extracted from 62 Canadian-grown two- and six-rowed barley cultivars and six American-grown six-rowed barley cultivars, were separated by polyacrylamide gel electrophoresis at acid pH. Band mobilities were shown to be reproducible within ± 0.005 relative mobility units. Hordein electrophoregram formulae were determined and catalogued for the 68 barley cultivars analyzed. Twenty-five of the cultivars produced unique electrophoregram formulae. The remaining 43 cultivars were divided into 17 groups, each containing between two and eight indistinguishable cultivars. Further analysis of electrophoregram formulae for Canadian-grown barley cultivars revealed that the majority of malting barley cultivars were distinguishable from feed barley cultivars. The usefulness of the acidic PAGE procedure for the identification of Canadian-grown barley cultivars is evaluated.

BARLEY CULTIVAR IDENTIFICATION BY SDS GRADIENT PAGE ANALYSIS OF HORDEIN

1987 ◽  
Vol 67 (4) ◽  
pp. 927-944 ◽  
Author(s):  
B. A. MARCHYLO
Keyword(s):  
Molecular Weight ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Resolving Power ◽  
Buffer System ◽  
Barley Cultivar ◽  
Protein Patterns ◽  
Barley Malt ◽  
Barley Cultivars

Sodium dodecyl sulfate gradient polyacrylamide gel electrophoresis (SDSGPAGE) was evaluated to determine whether it could provide improved resolving power of hordein proteins concomitant with improved discrimination (identification) of Canadian barley cultivars. Hordeins were subjected to electrophoresis using a linear gradient gel and a discontinuous buffer system. Proteins were detected using a silver-based color stain and gels were calibrated routinely for molecular weight determinations with a mixture of standard proteins. Molecular weight estimations of hordeins were performed by evaluation of the relationship between log (MW) versus log (R1) and reproducible linear calibration curves and molecular weight estimates for hordeins (CV 0.66%) were obtained. Densitometric analysis of protein band intensities revealed considerable variability in protein staining. Electrophoretic analysis of 100 barley cultivars revealed that, in general, resolution of SDSGPAGE was superior to that of acidic PAGE but considerable duplication of protein patterns among cultivars and their biotypes remained a problem. Cultivar formulae consisting of B, C and D hordein pattern designations were used to prepare a cultivar catalogue of protein patterns. Sixty-five formulae consisting of 30 B, 36 C and 3 D hordein patterns were obtained. SDSGPAGE also was found suitable for barley malt cultivar analysis.Key words: SDS gradient PAGE, barley, cultivar identification, hordein

IDENTIFICATION OF CULTIVARS OF FORAGE LEGUME (Desmodium ovalifolium GUILL ET PERR.) BY THEIR ELECTROPHORETIC PATTERNS

1987 ◽  
Vol 67 (3) ◽  
pp. 713-717 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
H. RAMIREZ ◽  
W. ROCA
Keyword(s):  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Forage Legume ◽  
Desmodium Ovalifolium ◽  
Electrophoretic Patterns ◽  
Electrophoretic Procedure

An electrophoretic procedure was developed for discriminating cultivars of Desmodium ovalifolium on the basis of patterns of partially purified seed proteins. Electrophoresis was done on uniform 15% polycrylamide gels in basic (8.9) pH. The method produced satisfactory discrimination of eight cultivars used in its initial evaluation.Key words: Forage legume, Desmodium ovalifolium Guill et Perr., cultivar identification, polyacrylamide gel electrophoresis

ALPHA AMYLASE DISTRIBUTION AND DDT RESPONSE IN CANADIAN BARLEY CULTIVARS

1971 ◽  
Vol 51 (5) ◽  
pp. 353-359 ◽  
Author(s):  
GEORGE FEDAK ◽  
TIBOR RAJHATHY
Keyword(s):  
Frequency Distribution ◽  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Foliar Spray ◽  
Alpha Amylase ◽  
Agar Gel ◽  
Barley Cultivars ◽  
Heat Stable ◽  
Agar Gel Electrophoresis

The heat-stable alpha amylase zymotype was studied by agar gel electrophoresis in 55 Canadian barley cultivars and most of their parents. A DC zymotype was found in 41 cultivars, DC1 in four, DC2C-DC polymorphism in nine and DC1-DC polymorphism in one. All cultivars were subjected to a foliar spray of DDT and all were found to be susceptible and monomorphic for this trait. These results are discussed in terms of cultivar identification, differences in frequency distribution of zymotypes between the European and Canadian material, and the introduction of these zymotypes into Canada.

Inheritance and distribution of variation at four avenin loci in North American oat germ plasm

Genome ◽  
1990 ◽  
Vol 33 (3) ◽  
pp. 416-424 ◽  
Author(s):  
E. Souza ◽  
M. E. Sorrells
Keyword(s):  
North American ◽  
Gel Electrophoresis ◽  
Germ Plasm ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
High Association ◽  
Electrophoretic Mobilities ◽  
Oat Cultivars ◽  
Taxonomic Studies

Avenins (prolamines of the Avena genus) have been shown to be useful in taxonomic studies and cultivar identification; specific allelic identification could assist in these types of studies as well as providing a basis for future linkage and gene mapping studies. The avenin patterns produced by nondenaturing polyacrylamide gel electrophoresis were compared in 70 North American oat cultivars and germ plasms. Populations of F2 progeny were subsequently evaluated to test for allelism of proteins found to be noncoincident in the survey of homozygous cultivars. A minimum of four loci (Av1, Av2, Av3, and Av4) were found to possess alternate alleles with distinctive electrophoretic mobilities. Segregation of 10 alternate alleles were observed in studies of F2 progeny: four for Av1, and two each for the other three loci. Additional variation found among the surveyed cultivars suggested at least two additional electrophoretically variant polypeptides. Several of the alleles were found to be associated with cultivars from specific geographic regions. Two examples were (i) the near exclusive association of the Av10.76 allele with Canadian cultivars and (ii) the high association of the Av10.58 allele with fall-planted cultivars. Fifty percent (SE ± 10.7%) of the fall-planted cultivars have the Av40.58 allele compared with 27.1% (SE ± 8.8%) of spring-planted cultivars.Key words: avenins, prolamines, polyacrylamide gel electrophoresis, linkage.

DISCRIMINATION OF CULTIVARS OF LENTIL (Lens culinaris Medic.) BY ELECTROPHORESIS OF SEED PROTEINS

1989 ◽  
Vol 69 (1) ◽  
pp. 243-246 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
K. W. CLARK
Keyword(s):  
Gel Electrophoresis ◽  
Lens Culinaris ◽  
Seed Protein ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel

Discrimination of lentil cultivars was achieved by analysis of seed protein by two types of polyacrylamide gel electrophoresis. Cultivars of lentil were discriminated by the presence or absence of diagnostic bands. Electrophoregrams of six seed lots of the cultivar Eston were identical and unaffected by growing conditions.Key words: Lens culinaris Medic, seed proteins, polyacrylamide gel electrophoresis, cultivar identification

scholarly journals Cathepsin G is a strong platelet agonist released by neutrophils

1988 ◽  
Vol 251 (1) ◽  
pp. 293-299 ◽  
Author(s):  
M A Selak ◽  
M Chignard ◽  
J B Smith
Keyword(s):  
Biological Activity ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Enzymic Activity ◽  
Calcium Mobilization ◽  
Cathepsin G ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Alpha 1 Antitrypsin ◽  
Acid Gel

The present studies were undertaken to characterize a serine protease released by N-formyl-L-Met-L-Leu-L-Phe (fMet-Leu-Phe)-stimulated neutrophils that rapidly induces platelet calcium mobilization, secretion and aggregation. The biological activity associated with this protease was unaffected by leupeptin, was only weakly diminished by N-p-tosyl-L-Lys-chloromethane, but was strongly inhibited by alpha 1-antitrypsin, soyabean trypsin inhibitor, N-tosyl-L-Phe-chloromethane and benzoyloxycarbonyl-Gly-Leu-Phe-chloromethane (Z-Gly-Leu-PheCH2Cl). These observations indicated that the biological activity of neutrophil supernatants could be attributed to a chymotrypsin-like enzyme such as cathepsin G. Furthermore, platelet aggregation and 5-hydroxytryptamine release induced by cell-free supernatants from fMet-Leu-Phe-stimulated neutrophils were found to be blocked by antiserum to cathepsin G in a concentration-dependent manner but were unaffected by antiserum to elastase. The biological activity present in neutrophil supernatants co-purified with enzymic activity for cathepsin G during sequential Aprotinin-Sepharose affinity chromatography and carboxymethyl-Sephadex chromatography. SDS/polyacrylamide-gel electrophoresis of the reduced, purified protein, demonstrated three polypeptides with apparent Mr values of 31,500, 29,000 and 28,000 and four polypeptides were resolved on acid-gel electrophoresis. Purified cathepsin G from neutrophils cross-reacted with anti-(cathepsin G) serum in a double immunodiffusion assay and elicited platelet calcium mobilization, 5-hydroxytryptamine secretion and aggregation. Calcium mobilization and secretion induced by low concentrations of cathepsin G were partially dependent on arachidonic acid metabolites and ADP, while stimulation by higher enzyme concentrations was independent of amplification pathways, indicating that cathepsin G is a strong platelet agonist. These results suggest that pathological processes which stimulate neutrophils and release cathepsin G can in turn result in the recruitment and activation of platelets.

Inheritance of novel high-molecular-weight glutenin subunits in the Tunisian bread wheat 'BT-2288'

Genome ◽  
1988 ◽  
Vol 30 (3) ◽  
pp. 442-445
Author(s):  
R. B. Gupta ◽  
K. W. Shepherd
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Wheat Cultivar ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Bread Making

Using sodium dodecyl sulphate-polyacrylamide gel electrophoresis, three new high-molecular-weight glutenin subunit/subunit combinations were detected in a Tunisian wheat cultivar (BT-2288) and these were designated bands 26, 7 + 11, and 5 + 9. Analysis of 112 testcross seeds revealed that the genes controlling them were additional alleles at Glu-A1, Glu-B1, and Glu-D1 loci, respectively. These alleles enhance the genetic variability available for cultivar identification and possibly for improving the bread-making quality of hexaploid wheat.Key words: Triticum aestivum, Glu-1 loci, high-molecular-weight glutenin subunits.

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