Associations between individual gliadin proteins and quality, agronomic and morphological attributes of wheat cultivars

1982 ◽  
Vol 33 (3) ◽  
pp. 409 ◽  
Author(s):  
CW Wrigley ◽  
PJ Robinson ◽  
WT Williams
Keyword(s):  
New Zealand ◽  
North America ◽  
Gel Electrophoresis ◽  
Spanning Tree ◽  
Minimum Spanning Tree ◽  
Starch Gel Electrophoresis ◽  
Wheat Cultivars ◽  
Morphological Attributes ◽  
Starch Gel ◽  
Gliadin Protein

The gliadin protein compositions of 79 wheat genotypes from Australia, New Zealand and North America, and one rye cultivar have been examined by starch gel electrophoresis. Interrelationships in the patterns thus obtained were investigated using a computer-generated inverse minimum spanning tree. Certain components were frequently found to occur together, presumably because their synthesis is controlled by closely linked genes. In addition, by using a network-generating program, associations between gliadins and many morphological (plant, head and grain), agronomic and quality attributes were studied. In many cases, specific gliadin components were found to be closely associated with certain attributes. In such cases a direct cause and effect cannot be inferred, but the approach indicates associations that warrant further study.

Identification of Australian wheat cultivars by laboratory procedures: examination of pure samples of grain

1974 ◽  
Vol 14 (71) ◽  
pp. 796 ◽  
Author(s):  
CW Wrigley ◽  
KW Shepherd
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Wheat Cultivars ◽  
Grain Hardness ◽  
Additional Information ◽  
Size Index ◽  
Starch Gel ◽  
Australian Wheat ◽  
Laboratory Procedures ◽  
Single Grain

Three laboratory procedures have been examined for the identification of about fifty wheat cultivars currently grown in Australia. The most discriminating of these methods is starch gel electrophoresis of gliadin proteins extracted from a single grain or from meal. This procedure is capable of identifying many of the cultivars directly. However, in some cases identification is complicated by the observation of more than one biotype for a cultivar on the basis of this test. By comparison, a larger number of grains can be examined by the qualitative phenol test but it is less discriminating. Additional information is provided by applying the test to glumes. Thirdly, quantitative assessment of grain hardness, measuring either particle size index or pearling resistance, gives a division of cultivars into about five groups. Specific results are listed for all methods so that the most suitable procedure can be chosen for distinguishing a particular group of cultivars.

Assessment of allozyme variation among New Zealand populations of Gracilaria chilensis (Gracialiares, Rhodophyta) using starch-gel electrophoresis

Hydrobiologia ◽  
1993 ◽  
Vol 260-261 (1) ◽  
pp. 159-165 ◽  
Author(s):  
Sompop Intasuwan ◽  
Margaret E. Gordon ◽  
Charles H. Daugherty ◽  
Graeme C. Lindsay
Keyword(s):  
New Zealand ◽  
Gel Electrophoresis ◽  
Allozyme Variation ◽  
Starch Gel Electrophoresis ◽  
Gracilaria Chilensis ◽  
Starch Gel

scholarly journals Isozymes for Cultivar Identification in Kiwifruit

HortScience ◽  
1991 ◽  
Vol 26 (7) ◽  
pp. 899-902 ◽  
Author(s):  
R. Messina ◽  
R. Testolin ◽  
M. Morgante
Keyword(s):  
New Zealand ◽  
Genetic Markers ◽  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Starch Gel Electrophoresis ◽  
Banding Patterns ◽  
Discriminating Power ◽  
Enzyme Systems ◽  
Starch Gel ◽  
Simultaneous Comparison

The usefulness of isozyme banding patterns as genetic markers in kiwifruit [Actinidia deliciosa (A. Chev.) C.F. Liang et A.R. Ferguson] was investigated using starch gel electrophoresis. Fifty-four entries putatively belonging to seven female and two male kiwifruit cultivars were examined for 13 enzyme systems (AAT, ACO, GDH, G6PDH, IDH, MDH, ME, MNR, NDH, 6PGD, PGI, PGM, and SKDH). Four enzyme systems, ACO, MDH, NDH, and SKDH, showed identical banding patterns in all clones surveyed. Of the remaining enzymes, AAT, PGI, and PGM had the best discriminating power. Six enzyme systems (GDH, G6PDH, IDH, ME, MNR, and 6PGD), though showing polymorphic banding patterns, were poorly resolved. All the New Zealand cultivars were uniquely identified by the simultaneous comparison of the AAT, PGI, and PGM zymograms. Some enzyme systems were also polymorphic among plants within the same cultivar, thus proving the heterogeneity of kiwifruit material introduced into Europe in the early 1970s.

scholarly journals CHARACTERISTICS OF STREPTOCOCCAL GROUP-SPECIFIC ANTIBODY ISOLATED FROM HYPERIMMUNE RABBITS

1966 ◽  
Vol 123 (4) ◽  
pp. 599-614 ◽  
Author(s):  
C. Kirk Osterland ◽  
Edward J. Miller ◽  
Walter W. Karakawa ◽  
Richard M. Krause
Keyword(s):  
New Zealand ◽  
Specific Antibody ◽  
Gel Electrophoresis ◽  
Limited Range ◽  
Carbohydrate Antigen ◽  
Starch Gel Electrophoresis ◽  
Normal Complement ◽  
Zone Electrophoresis ◽  
Group A ◽  
Starch Gel

Intravenous immunization of New Zealand red rabbits with streptococcal group-specific bacterial vaccines yielded sera which possessed markedly elevated γ-globulin. The sera of one rabbit immunized with Group A-variant vaccine possessed 55 mg/ml of γ-globulin. The bulk of this γ-globulin, identified as γG-globulin, was homogeneous by zone electrophoresis and of specificity directed against the Group A-variant carbohydrate antigen. L chains isolated from specific antibody obtained from an immune precipitate were distributed as a single band on starch gel electrophoresis, whereas the normal γ-globulin traveled as a diffuse smear. These data suggest that the rabbit streptococcal Group A-variant antibodies possess a limited range of physicochemical properties and electrophoretic mobility compared to that generally observed for the normal complement of γ-globulin.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

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