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.

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

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

Polyacrylamide Gel Electrophoresis for Cultivar Identification in Tobacco 1

Crop Science ◽  
1985 ◽  
Vol 25 (6) ◽  
pp. 971-974 ◽  
Author(s):  
C. A. Wilkinson ◽  
C. L. Mulchi ◽  
M. K. Aycock
Keyword(s):  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel

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.

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.

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